Abstract

Micro-scale, non-invasive, three-dimensional cross-sectional imaging of protein crystals was successfully accomplished using ultra-high resolution optical coherence tomography (UHR-OCT) with low noise, Gaussian like supercontinuum. This technique facilitated visualization of protein crystals even those in medium that also contained substantial amounts of precipitates. We found the enhancement of the scattered signal from protein crystal by inclusion of agarose gel in the crystallization medium. Crystals of a protein and a salt in the same sample when visualized by UHR-OCT showed distinct physical characteristics, suggesting that protein and salt crystals may, in general, be distinguishable by UHR-OCT. UHR-OCT is a nondestructive and rapid method, which should therefore find use in automated systems designed to visualize crystals.

© 2012 OSA

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2012 (1)

2011 (1)

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

2010 (1)

M. Nishiura, T. Kobayashi, M. Adachi, J. Nakanishi, T. Ueno, Y. Ito, and N. Nishizawa, “In vivo ultrahigh-resolution ophthalmic optical coherence tomography using Gaussian-shaped super continuum,” Jpn. J. Appl. Phys. 49(1), 012701 (2010).
[CrossRef]

2009 (4)

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

2008 (1)

J. J. Kehoe, G. E. Remondetto, M. Subirade, E. R. Morris, and A. Brodkorb, “Tryptophan-mediated denaturation of beta-lactoglobulin A by UV irradiation,” J. Agric. Food Chem. 56(12), 4720–4725 (2008).
[CrossRef] [PubMed]

2005 (1)

R. A. Judge, K. Swift, and C. González, “An ultraviolet fluorescence-based method for identifying and distinguishing protein crystals,” Acta Crystallogr. D Biol. Crystallogr. 61(1), 60–66 (2005).
[CrossRef] [PubMed]

2003 (1)

D. Kobayashi, M. Tamoi, T. Iwaki, S. Shigeoka, and A. Wadano, “Molecular characterization and redox regulation of phosphoribulokinase from the cyanobacterium Synechococcus sp. PCC 7942,” Plant Cell Physiol. 44(3), 269–276 (2003).
[CrossRef] [PubMed]

2002 (3)

J. A. Gavira and J. M. García-Ruiz, “Agarose as crystallisation media for proteins II: trapping of gel fibres into the crystals,” Acta Crystallogr. D Biol. Crystallogr. 58(10), 1653–1656 (2002).
[CrossRef] [PubMed]

C. Sauter, B. Lorber, and R. Giegé, “Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature,” Proteins 48(2), 146–150 (2002).
[CrossRef] [PubMed]

C. Biertümpfel, J. Basquin, D. Suck, and C. Sauter, “Crystallization of biological macromolecules using agarose gel,” Acta Crystallogr. D Biol. Crystallogr. 58(10), 1657–1659 (2002).
[CrossRef] [PubMed]

2001 (1)

W. Drexler, U. Morgner, R. K. Ghanta, F. X. Kärtner, J. S. Schuman, and J. G. Fujimoto, “Ultrahigh-resolution ophthalmic optical coherence tomography,” Nat. Med. 7(4), 502–507 (2001).
[CrossRef] [PubMed]

1999 (2)

B. Lorber, C. Sauter, M. C. Robert, B. Capelle, and R. Giegé, “Crystallization within agarose gel in microgravity improves the quality of thaumatin crystals,” Acta Crystallogr. D Biol. Crystallogr. 55(9), 1491–1494 (1999).
[CrossRef] [PubMed]

J. P. Dunkers, R. S. Parnas, C. G. Zimba, R. S. Peterson, K. M. Flynn, J. G. Fujimoto, and B. E. Bouma, “Optical coherence tomography of glass reinforced polymer composites,” Compos., Part A Appl. Sci. Manuf. 30, 139–145 (1999).
[CrossRef]

1997 (1)

N. Pernodet, M. Maaloum, and B. Tinland, “Pore size of agarose gels by atomic force microscopy,” Electrophoresis 18(1), 55–58 (1997).
[CrossRef] [PubMed]

1995 (1)

A. Wadano, Y. Kamata, T. Iwaki, K. Nishikawa, and T. Hirahashi, “Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942,” Plant Cell Physiol. 36(7), 1381–1385 (1995).
[PubMed]

1994 (1)

K. J. Thiessen, “The use of two novel methods to grow protein crystals by microdialysis and vapor diffusion in an agarose gel,” Acta Crystallogr. D Biol. Crystallogr. 50(4), 491–495 (1994).
[CrossRef] [PubMed]

1991 (1)

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

Adachi, H.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

Adachi, M.

M. Nishiura, T. Kobayashi, M. Adachi, J. Nakanishi, T. Ueno, Y. Ito, and N. Nishizawa, “In vivo ultrahigh-resolution ophthalmic optical coherence tomography using Gaussian-shaped super continuum,” Jpn. J. Appl. Phys. 49(1), 012701 (2010).
[CrossRef]

Basquin, J.

C. Biertümpfel, J. Basquin, D. Suck, and C. Sauter, “Crystallization of biological macromolecules using agarose gel,” Acta Crystallogr. D Biol. Crystallogr. 58(10), 1657–1659 (2002).
[CrossRef] [PubMed]

Biertümpfel, C.

C. Biertümpfel, J. Basquin, D. Suck, and C. Sauter, “Crystallization of biological macromolecules using agarose gel,” Acta Crystallogr. D Biol. Crystallogr. 58(10), 1657–1659 (2002).
[CrossRef] [PubMed]

Bouma, B. E.

J. P. Dunkers, R. S. Parnas, C. G. Zimba, R. S. Peterson, K. M. Flynn, J. G. Fujimoto, and B. E. Bouma, “Optical coherence tomography of glass reinforced polymer composites,” Compos., Part A Appl. Sci. Manuf. 30, 139–145 (1999).
[CrossRef]

Brodkorb, A.

J. J. Kehoe, G. E. Remondetto, M. Subirade, E. R. Morris, and A. Brodkorb, “Tryptophan-mediated denaturation of beta-lactoglobulin A by UV irradiation,” J. Agric. Food Chem. 56(12), 4720–4725 (2008).
[CrossRef] [PubMed]

Capelle, B.

B. Lorber, C. Sauter, M. C. Robert, B. Capelle, and R. Giegé, “Crystallization within agarose gel in microgravity improves the quality of thaumatin crystals,” Acta Crystallogr. D Biol. Crystallogr. 55(9), 1491–1494 (1999).
[CrossRef] [PubMed]

Chang, W.

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

Drexler, W.

W. Drexler, U. Morgner, R. K. Ghanta, F. X. Kärtner, J. S. Schuman, and J. G. Fujimoto, “Ultrahigh-resolution ophthalmic optical coherence tomography,” Nat. Med. 7(4), 502–507 (2001).
[CrossRef] [PubMed]

Dunkers, J. P.

J. P. Dunkers, R. S. Parnas, C. G. Zimba, R. S. Peterson, K. M. Flynn, J. G. Fujimoto, and B. E. Bouma, “Optical coherence tomography of glass reinforced polymer composites,” Compos., Part A Appl. Sci. Manuf. 30, 139–145 (1999).
[CrossRef]

Flotte, T.

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

Flynn, K. M.

J. P. Dunkers, R. S. Parnas, C. G. Zimba, R. S. Peterson, K. M. Flynn, J. G. Fujimoto, and B. E. Bouma, “Optical coherence tomography of glass reinforced polymer composites,” Compos., Part A Appl. Sci. Manuf. 30, 139–145 (1999).
[CrossRef]

Fujimoto, J. G.

W. Drexler, U. Morgner, R. K. Ghanta, F. X. Kärtner, J. S. Schuman, and J. G. Fujimoto, “Ultrahigh-resolution ophthalmic optical coherence tomography,” Nat. Med. 7(4), 502–507 (2001).
[CrossRef] [PubMed]

J. P. Dunkers, R. S. Parnas, C. G. Zimba, R. S. Peterson, K. M. Flynn, J. G. Fujimoto, and B. E. Bouma, “Optical coherence tomography of glass reinforced polymer composites,” Compos., Part A Appl. Sci. Manuf. 30, 139–145 (1999).
[CrossRef]

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

García-Ruiz, J. M.

J. A. Gavira and J. M. García-Ruiz, “Agarose as crystallisation media for proteins II: trapping of gel fibres into the crystals,” Acta Crystallogr. D Biol. Crystallogr. 58(10), 1653–1656 (2002).
[CrossRef] [PubMed]

Gavira, J. A.

J. A. Gavira and J. M. García-Ruiz, “Agarose as crystallisation media for proteins II: trapping of gel fibres into the crystals,” Acta Crystallogr. D Biol. Crystallogr. 58(10), 1653–1656 (2002).
[CrossRef] [PubMed]

Ghanta, R. K.

W. Drexler, U. Morgner, R. K. Ghanta, F. X. Kärtner, J. S. Schuman, and J. G. Fujimoto, “Ultrahigh-resolution ophthalmic optical coherence tomography,” Nat. Med. 7(4), 502–507 (2001).
[CrossRef] [PubMed]

Giegé, R.

C. Sauter, B. Lorber, and R. Giegé, “Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature,” Proteins 48(2), 146–150 (2002).
[CrossRef] [PubMed]

B. Lorber, C. Sauter, M. C. Robert, B. Capelle, and R. Giegé, “Crystallization within agarose gel in microgravity improves the quality of thaumatin crystals,” Acta Crystallogr. D Biol. Crystallogr. 55(9), 1491–1494 (1999).
[CrossRef] [PubMed]

González, C.

R. A. Judge, K. Swift, and C. González, “An ultraviolet fluorescence-based method for identifying and distinguishing protein crystals,” Acta Crystallogr. D Biol. Crystallogr. 61(1), 60–66 (2005).
[CrossRef] [PubMed]

Gregory, K.

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

Hasenaka, H.

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

Hee, M. R.

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

Hirahashi, T.

A. Wadano, Y. Kamata, T. Iwaki, K. Nishikawa, and T. Hirahashi, “Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942,” Plant Cell Physiol. 36(7), 1381–1385 (1995).
[PubMed]

Hirose, M.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

Huang, D.

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

Inoue, T.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

Ishida, S.

Ito, Y.

M. Nishiura, T. Kobayashi, M. Adachi, J. Nakanishi, T. Ueno, Y. Ito, and N. Nishizawa, “In vivo ultrahigh-resolution ophthalmic optical coherence tomography using Gaussian-shaped super continuum,” Jpn. J. Appl. Phys. 49(1), 012701 (2010).
[CrossRef]

Iwaki, T.

D. Kobayashi, M. Tamoi, T. Iwaki, S. Shigeoka, and A. Wadano, “Molecular characterization and redox regulation of phosphoribulokinase from the cyanobacterium Synechococcus sp. PCC 7942,” Plant Cell Physiol. 44(3), 269–276 (2003).
[CrossRef] [PubMed]

A. Wadano, Y. Kamata, T. Iwaki, K. Nishikawa, and T. Hirahashi, “Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942,” Plant Cell Physiol. 36(7), 1381–1385 (1995).
[PubMed]

Judge, R. A.

R. A. Judge, K. Swift, and C. González, “An ultraviolet fluorescence-based method for identifying and distinguishing protein crystals,” Acta Crystallogr. D Biol. Crystallogr. 61(1), 60–66 (2005).
[CrossRef] [PubMed]

Kamata, Y.

A. Wadano, Y. Kamata, T. Iwaki, K. Nishikawa, and T. Hirahashi, “Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942,” Plant Cell Physiol. 36(7), 1381–1385 (1995).
[PubMed]

Kärtner, F. X.

W. Drexler, U. Morgner, R. K. Ghanta, F. X. Kärtner, J. S. Schuman, and J. G. Fujimoto, “Ultrahigh-resolution ophthalmic optical coherence tomography,” Nat. Med. 7(4), 502–507 (2001).
[CrossRef] [PubMed]

Kehoe, J. J.

J. J. Kehoe, G. E. Remondetto, M. Subirade, E. R. Morris, and A. Brodkorb, “Tryptophan-mediated denaturation of beta-lactoglobulin A by UV irradiation,” J. Agric. Food Chem. 56(12), 4720–4725 (2008).
[CrossRef] [PubMed]

Kitatani, T.

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

Kobayashi, D.

D. Kobayashi, M. Tamoi, T. Iwaki, S. Shigeoka, and A. Wadano, “Molecular characterization and redox regulation of phosphoribulokinase from the cyanobacterium Synechococcus sp. PCC 7942,” Plant Cell Physiol. 44(3), 269–276 (2003).
[CrossRef] [PubMed]

Kobayashi, T.

M. Nishiura, T. Kobayashi, M. Adachi, J. Nakanishi, T. Ueno, Y. Ito, and N. Nishizawa, “In vivo ultrahigh-resolution ophthalmic optical coherence tomography using Gaussian-shaped super continuum,” Jpn. J. Appl. Phys. 49(1), 012701 (2010).
[CrossRef]

Lin, C. P.

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

Lorber, B.

C. Sauter, B. Lorber, and R. Giegé, “Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature,” Proteins 48(2), 146–150 (2002).
[CrossRef] [PubMed]

B. Lorber, C. Sauter, M. C. Robert, B. Capelle, and R. Giegé, “Crystallization within agarose gel in microgravity improves the quality of thaumatin crystals,” Acta Crystallogr. D Biol. Crystallogr. 55(9), 1491–1494 (1999).
[CrossRef] [PubMed]

Maaloum, M.

N. Pernodet, M. Maaloum, and B. Tinland, “Pore size of agarose gels by atomic force microscopy,” Electrophoresis 18(1), 55–58 (1997).
[CrossRef] [PubMed]

Maruyama, M.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

Matsumura, H.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

Mizohata, E.

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

Morgner, U.

W. Drexler, U. Morgner, R. K. Ghanta, F. X. Kärtner, J. S. Schuman, and J. G. Fujimoto, “Ultrahigh-resolution ophthalmic optical coherence tomography,” Nat. Med. 7(4), 502–507 (2001).
[CrossRef] [PubMed]

Mori, Y.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

Morris, E. R.

J. J. Kehoe, G. E. Remondetto, M. Subirade, E. R. Morris, and A. Brodkorb, “Tryptophan-mediated denaturation of beta-lactoglobulin A by UV irradiation,” J. Agric. Food Chem. 56(12), 4720–4725 (2008).
[CrossRef] [PubMed]

Murai, R.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

Murakami, S.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

Nakanishi, J.

M. Nishiura, T. Kobayashi, M. Adachi, J. Nakanishi, T. Ueno, Y. Ito, and N. Nishizawa, “In vivo ultrahigh-resolution ophthalmic optical coherence tomography using Gaussian-shaped super continuum,” Jpn. J. Appl. Phys. 49(1), 012701 (2010).
[CrossRef]

Niiyama, M.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

Nishikawa, K.

A. Wadano, Y. Kamata, T. Iwaki, K. Nishikawa, and T. Hirahashi, “Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942,” Plant Cell Physiol. 36(7), 1381–1385 (1995).
[PubMed]

Nishiura, M.

M. Nishiura, T. Kobayashi, M. Adachi, J. Nakanishi, T. Ueno, Y. Ito, and N. Nishizawa, “In vivo ultrahigh-resolution ophthalmic optical coherence tomography using Gaussian-shaped super continuum,” Jpn. J. Appl. Phys. 49(1), 012701 (2010).
[CrossRef]

Nishizawa, N.

S. Ishida and N. Nishizawa, “Quantitative comparison of contrast and imaging depth of ultrahigh-resolution optical coherence tomography images in 800-1700 nm wavelength region,” Biomed. Opt. Express 3(2), 282–294 (2012).
[CrossRef] [PubMed]

M. Nishiura, T. Kobayashi, M. Adachi, J. Nakanishi, T. Ueno, Y. Ito, and N. Nishizawa, “In vivo ultrahigh-resolution ophthalmic optical coherence tomography using Gaussian-shaped super continuum,” Jpn. J. Appl. Phys. 49(1), 012701 (2010).
[CrossRef]

Parnas, R. S.

J. P. Dunkers, R. S. Parnas, C. G. Zimba, R. S. Peterson, K. M. Flynn, J. G. Fujimoto, and B. E. Bouma, “Optical coherence tomography of glass reinforced polymer composites,” Compos., Part A Appl. Sci. Manuf. 30, 139–145 (1999).
[CrossRef]

Pernodet, N.

N. Pernodet, M. Maaloum, and B. Tinland, “Pore size of agarose gels by atomic force microscopy,” Electrophoresis 18(1), 55–58 (1997).
[CrossRef] [PubMed]

Peterson, R. S.

J. P. Dunkers, R. S. Parnas, C. G. Zimba, R. S. Peterson, K. M. Flynn, J. G. Fujimoto, and B. E. Bouma, “Optical coherence tomography of glass reinforced polymer composites,” Compos., Part A Appl. Sci. Manuf. 30, 139–145 (1999).
[CrossRef]

Puliafito, C. A.

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

Remondetto, G. E.

J. J. Kehoe, G. E. Remondetto, M. Subirade, E. R. Morris, and A. Brodkorb, “Tryptophan-mediated denaturation of beta-lactoglobulin A by UV irradiation,” J. Agric. Food Chem. 56(12), 4720–4725 (2008).
[CrossRef] [PubMed]

Robert, M. C.

B. Lorber, C. Sauter, M. C. Robert, B. Capelle, and R. Giegé, “Crystallization within agarose gel in microgravity improves the quality of thaumatin crystals,” Acta Crystallogr. D Biol. Crystallogr. 55(9), 1491–1494 (1999).
[CrossRef] [PubMed]

Sauter, C.

C. Sauter, B. Lorber, and R. Giegé, “Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature,” Proteins 48(2), 146–150 (2002).
[CrossRef] [PubMed]

C. Biertümpfel, J. Basquin, D. Suck, and C. Sauter, “Crystallization of biological macromolecules using agarose gel,” Acta Crystallogr. D Biol. Crystallogr. 58(10), 1657–1659 (2002).
[CrossRef] [PubMed]

B. Lorber, C. Sauter, M. C. Robert, B. Capelle, and R. Giegé, “Crystallization within agarose gel in microgravity improves the quality of thaumatin crystals,” Acta Crystallogr. D Biol. Crystallogr. 55(9), 1491–1494 (1999).
[CrossRef] [PubMed]

Sazaki, G.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

Schuman, J. S.

W. Drexler, U. Morgner, R. K. Ghanta, F. X. Kärtner, J. S. Schuman, and J. G. Fujimoto, “Ultrahigh-resolution ophthalmic optical coherence tomography,” Nat. Med. 7(4), 502–507 (2001).
[CrossRef] [PubMed]

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

Shigeoka, S.

D. Kobayashi, M. Tamoi, T. Iwaki, S. Shigeoka, and A. Wadano, “Molecular characterization and redox regulation of phosphoribulokinase from the cyanobacterium Synechococcus sp. PCC 7942,” Plant Cell Physiol. 44(3), 269–276 (2003).
[CrossRef] [PubMed]

Shimizu, N.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

Stinson, W. G.

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

Subirade, M.

J. J. Kehoe, G. E. Remondetto, M. Subirade, E. R. Morris, and A. Brodkorb, “Tryptophan-mediated denaturation of beta-lactoglobulin A by UV irradiation,” J. Agric. Food Chem. 56(12), 4720–4725 (2008).
[CrossRef] [PubMed]

Suck, D.

C. Biertümpfel, J. Basquin, D. Suck, and C. Sauter, “Crystallization of biological macromolecules using agarose gel,” Acta Crystallogr. D Biol. Crystallogr. 58(10), 1657–1659 (2002).
[CrossRef] [PubMed]

Sugiyama, S.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

Swanson, E. A.

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

Swift, K.

R. A. Judge, K. Swift, and C. González, “An ultraviolet fluorescence-based method for identifying and distinguishing protein crystals,” Acta Crystallogr. D Biol. Crystallogr. 61(1), 60–66 (2005).
[CrossRef] [PubMed]

Takahashi, Y.

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

Takano, K.

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

Tamoi, M.

D. Kobayashi, M. Tamoi, T. Iwaki, S. Shigeoka, and A. Wadano, “Molecular characterization and redox regulation of phosphoribulokinase from the cyanobacterium Synechococcus sp. PCC 7942,” Plant Cell Physiol. 44(3), 269–276 (2003).
[CrossRef] [PubMed]

Tanabe, K.

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

Thiessen, K. J.

K. J. Thiessen, “The use of two novel methods to grow protein crystals by microdialysis and vapor diffusion in an agarose gel,” Acta Crystallogr. D Biol. Crystallogr. 50(4), 491–495 (1994).
[CrossRef] [PubMed]

Tinland, B.

N. Pernodet, M. Maaloum, and B. Tinland, “Pore size of agarose gels by atomic force microscopy,” Electrophoresis 18(1), 55–58 (1997).
[CrossRef] [PubMed]

Ueno, T.

M. Nishiura, T. Kobayashi, M. Adachi, J. Nakanishi, T. Ueno, Y. Ito, and N. Nishizawa, “In vivo ultrahigh-resolution ophthalmic optical coherence tomography using Gaussian-shaped super continuum,” Jpn. J. Appl. Phys. 49(1), 012701 (2010).
[CrossRef]

Wadano, A.

D. Kobayashi, M. Tamoi, T. Iwaki, S. Shigeoka, and A. Wadano, “Molecular characterization and redox regulation of phosphoribulokinase from the cyanobacterium Synechococcus sp. PCC 7942,” Plant Cell Physiol. 44(3), 269–276 (2003).
[CrossRef] [PubMed]

A. Wadano, Y. Kamata, T. Iwaki, K. Nishikawa, and T. Hirahashi, “Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942,” Plant Cell Physiol. 36(7), 1381–1385 (1995).
[PubMed]

Zimba, C. G.

J. P. Dunkers, R. S. Parnas, C. G. Zimba, R. S. Peterson, K. M. Flynn, J. G. Fujimoto, and B. E. Bouma, “Optical coherence tomography of glass reinforced polymer composites,” Compos., Part A Appl. Sci. Manuf. 30, 139–145 (1999).
[CrossRef]

Acta Crystallogr. D Biol. Crystallogr. (5)

R. A. Judge, K. Swift, and C. González, “An ultraviolet fluorescence-based method for identifying and distinguishing protein crystals,” Acta Crystallogr. D Biol. Crystallogr. 61(1), 60–66 (2005).
[CrossRef] [PubMed]

C. Biertümpfel, J. Basquin, D. Suck, and C. Sauter, “Crystallization of biological macromolecules using agarose gel,” Acta Crystallogr. D Biol. Crystallogr. 58(10), 1657–1659 (2002).
[CrossRef] [PubMed]

B. Lorber, C. Sauter, M. C. Robert, B. Capelle, and R. Giegé, “Crystallization within agarose gel in microgravity improves the quality of thaumatin crystals,” Acta Crystallogr. D Biol. Crystallogr. 55(9), 1491–1494 (1999).
[CrossRef] [PubMed]

K. J. Thiessen, “The use of two novel methods to grow protein crystals by microdialysis and vapor diffusion in an agarose gel,” Acta Crystallogr. D Biol. Crystallogr. 50(4), 491–495 (1994).
[CrossRef] [PubMed]

J. A. Gavira and J. M. García-Ruiz, “Agarose as crystallisation media for proteins II: trapping of gel fibres into the crystals,” Acta Crystallogr. D Biol. Crystallogr. 58(10), 1653–1656 (2002).
[CrossRef] [PubMed]

Appl. Phys. Express (1)

K. Tanabe, M. Hirose, R. Murai, S. Sugiyama, N. Shimizu, M. Maruyama, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, E. Mizohata, T. Inoue, and H. Matsumura, “Promotion of crystal nucleation of protein by semi-solid Agarose gel,” Appl. Phys. Express 2(12), 125501 (2009).
[CrossRef]

Biomed. Opt. Express (1)

Compos., Part A Appl. Sci. Manuf. (1)

J. P. Dunkers, R. S. Parnas, C. G. Zimba, R. S. Peterson, K. M. Flynn, J. G. Fujimoto, and B. E. Bouma, “Optical coherence tomography of glass reinforced polymer composites,” Compos., Part A Appl. Sci. Manuf. 30, 139–145 (1999).
[CrossRef]

Electrophoresis (1)

N. Pernodet, M. Maaloum, and B. Tinland, “Pore size of agarose gels by atomic force microscopy,” Electrophoresis 18(1), 55–58 (1997).
[CrossRef] [PubMed]

J. Agric. Food Chem. (1)

J. J. Kehoe, G. E. Remondetto, M. Subirade, E. R. Morris, and A. Brodkorb, “Tryptophan-mediated denaturation of beta-lactoglobulin A by UV irradiation,” J. Agric. Food Chem. 56(12), 4720–4725 (2008).
[CrossRef] [PubMed]

J. Cryst. Growth (1)

H. Hasenaka, S. Sugiyama, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of protein crystals grown in agarose gel,” J. Cryst. Growth 312(1), 73–78 (2009).
[CrossRef]

Jpn. J. Appl. Phys. (4)

S. Sugiyama, M. Hirose, N. Shimizu, M. Niiyama, M. Maruyama, G. Sazaki, R. Murai, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel,” Jpn. J. Appl. Phys. 50(2), 025502 (2011).
[CrossRef]

S. Sugiyama, H. Hasenaka, M. Hirose, N. Shimizu, T. Kitatani, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, and H. Matsumura, “Femtosecond laser processing of Agarose gel surrounding protein crystals for development of an automated Crystal capturing system,” Jpn. J. Appl. Phys. 48(10), 105502 (2009).
[CrossRef]

S. Sugiyama, K. Tanabe, M. Hirose, T. Kitatani, H. Hasenaka, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, Y. Mori, T. Inoue, and H. Matsumura, “Protein crystallization in Agarose gel with high strength: developing an automated system for protein crystallographic processes,” Jpn. J. Appl. Phys. 48(7), 075502 (2009).
[CrossRef]

M. Nishiura, T. Kobayashi, M. Adachi, J. Nakanishi, T. Ueno, Y. Ito, and N. Nishizawa, “In vivo ultrahigh-resolution ophthalmic optical coherence tomography using Gaussian-shaped super continuum,” Jpn. J. Appl. Phys. 49(1), 012701 (2010).
[CrossRef]

Nat. Med. (1)

W. Drexler, U. Morgner, R. K. Ghanta, F. X. Kärtner, J. S. Schuman, and J. G. Fujimoto, “Ultrahigh-resolution ophthalmic optical coherence tomography,” Nat. Med. 7(4), 502–507 (2001).
[CrossRef] [PubMed]

Plant Cell Physiol. (2)

D. Kobayashi, M. Tamoi, T. Iwaki, S. Shigeoka, and A. Wadano, “Molecular characterization and redox regulation of phosphoribulokinase from the cyanobacterium Synechococcus sp. PCC 7942,” Plant Cell Physiol. 44(3), 269–276 (2003).
[CrossRef] [PubMed]

A. Wadano, Y. Kamata, T. Iwaki, K. Nishikawa, and T. Hirahashi, “Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942,” Plant Cell Physiol. 36(7), 1381–1385 (1995).
[PubMed]

Proteins (1)

C. Sauter, B. Lorber, and R. Giegé, “Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature,” Proteins 48(2), 146–150 (2002).
[CrossRef] [PubMed]

Science (1)

D. Huang, E. A. Swanson, C. P. Lin, J. S. Schuman, W. G. Stinson, W. Chang, M. R. Hee, T. Flotte, K. Gregory, C. A. Puliafito, and J. G. Fujimoto, “Optical coherence tomography,” Science 254(5035), 1178–1181 (1991).
[CrossRef] [PubMed]

Other (3)

B. E. Bouma and G. J. Tearney, Handbook of Optical Coherence Tomography (Marcel Dekker, 2002)

W. Drexler and J. G. Fujimoto, Optical Coherence Tomography (Springer, 2008).

J. G. Fujimoto, A. D. Aguirre, Y. Chen, P. R. Herz, P.-L. Hsiung, T. H. Ko, N. Nishizawa, and F. X. Kartner, Ultrashort Laser Pulses in Biology and Medicine (Springer, 2007), Chap. 1.

Supplementary Material (3)

» Media 1: MOV (3829 KB)     
» Media 2: MOV (3999 KB)     
» Media 3: MOV (3903 KB)     

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Figures (4)

Fig. 1
Fig. 1

(a) Experimental setup of 3D imaging of protein crystals using UHR-OCT with SC, (b) example of light micrograph of protein crystals, (c) example of picture of protein crystal taken with CCD camera when the aiming beam was irradiated. SC: supercontinuum, PC: polarization controller.

Fig. 2
Fig. 2

Cross sections of three-dimensional UHR-OCT images of HEWL crystals grown in (a) 0.0, (b) 0.4, (c) 0.8, (d) 1.2, and (e) 1.8% (w/v) agarose. (f) An image of a drop that contained Synechococcus phosphoribulokinase crystals and 1.0% (w/v) agarose. The crystals shown in panels (e) and (f) are clearly and non-invasively seen at μm resolution. Media 1 shows the 3D UHR-OCT image of HEWL crystals grown in the same condition as that for Fig. 2(e).

Fig. 3
Fig. 3

(a) Light micrograph. The HEWL crystal, circled in red, is difficult to see because it is surrounded by aggregates and amorphous material. (b) Cross section of a three-dimensional UHR-OCT image. The protein crystal is circled in red. The aggregates and amorphous material are colored black. The cross section is a still from Media 2.

Fig. 4
Fig. 4

(a) Light micrograph. Differentiating between the HEWL crystal and the calcium phosphate crystal is difficult. (b) Cross section of a three-dimensional UHR-OCT image. The red arrow points the calcium phosphate crystal and the blue arrow points the HEWL crystal. The difference in the signal intensities provides a better means of differentiating between the HEWL crystal and the calcium phosphate crystal. Media 3 shows the 3D UHR-OCT image of HEWL crystals and the calcium phosphate crystal.

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