메뉴 건너뛰기




Volumn 14, Issue 3, 2003, Pages 13-16

The Space Experiment of Protein Crystallization aboard the Chinese Spacecraft SZ-3

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL GROWTH; CRYSTALLIZATION; DIFFUSION; MICROGRAVITY PROCESSING; MORPHOLOGY; SPACECRAFT; X RAY DIFFRACTION;

EID: 1542500934     PISSN: 09380108     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02870939     Document Type: Conference Paper
Times cited : (6)

References (23)
  • 1
    • 0035502112 scopus 로고    scopus 로고
    • Towards Protein Crystal Growth on the International Space Station-Innovative Tools, Diagnostics and Applications
    • Stapelmann, J., Smolik, G., Lautenschlager, P., et al.: Towards Protein Crystal Growth on the International Space Station-Innovative Tools, Diagnostics and Applications, J. Crystal Growth, vol. 232 (1-4), p468 (2001).
    • (2001) J. Crystal Growth , vol.232 , Issue.1-4 , pp. 468
    • Stapelmann, J.1    Smolik, G.2    Lautenschlager, P.3
  • 2
    • 0034898172 scopus 로고    scopus 로고
    • A Test of Macromolecular Crystallization in Microgravity: Large Well-ordered Insulin Crystals
    • Borgstahl, G.E., Vahedi-Faridi, A., Lovelace, J., Bellamy, H.D., Snell, E.H.: A Test of Macromolecular Crystallization in Microgravity: Large Well-ordered Insulin Crystals, Acta Cryst. (D), vol. 57 (Pt 8), p1204 (2001).
    • (2001) Acta Cryst. (D) , vol.57 , Issue.PART 8 , pp. 1204
    • Borgstahl, G.E.1    Vahedi-Faridi, A.2    Lovelace, J.3    Bellamy, H.D.4    Snell, E.H.5
  • 3
    • 0036005618 scopus 로고    scopus 로고
    • Comparative Analysis of Space-grown and Earth-grown Crystals of an Aminoacyl-tRNA Synthetase: Space-grown Crystals are More Useful for Structural Determination
    • Ng, J.D., Sauter, C., Lorber, B., Kirkland, N., Arnez, J., Giege, R.: Comparative Analysis of Space-grown and Earth-grown Crystals of an Aminoacyl-tRNA Synthetase: Space-grown Crystals are More Useful for Structural Determination, Acta Cryst. (D), vol. 58 (Pt 4), p645 (2002).
    • (2002) Acta Cryst. (D) , vol.58 , Issue.PART 4 , pp. 645
    • Ng, J.D.1    Sauter, C.2    Lorber, B.3    Kirkland, N.4    Arnez, J.5    Giege, R.6
  • 6
    • 0030251602 scopus 로고    scopus 로고
    • The Second Space Experiment of Protein Crystallization with Domestic Facilities
    • Wang, Y.-P., Pan, J.-S., Han, Y., Bi, R.-C, et al.: The Second Space Experiment of Protein Crystallization with Domestic Facilities, Science in China, Ser. C, vol. 39 (5), p458 (1996).
    • (1996) Science in China, Ser. C , vol.39 , Issue.5 , pp. 458
    • Wang, Y.-P.1    Pan, J.-S.2    Han, Y.3    Bi, R.-C.4
  • 8
    • 0344809373 scopus 로고    scopus 로고
    • A Facility of Double Temperatures and Double Chambers for Protein Crystal Growth in Space
    • Pang, S., Fu, K., Ju, G., Wang, X., Gui, W.: A Facility of Double Temperatures and Double Chambers for Protein Crystal Growth in Space, Chin. J. Space Science, vol. 19 (Suppl.), p109 (1999).
    • (1999) Chin. J. Space Science , vol.19 , Issue.SUPPL. , pp. 109
    • Pang, S.1    Fu, K.2    Ju, G.3    Wang, X.4    Gui, W.5
  • 9
    • 0035001144 scopus 로고    scopus 로고
    • Human Dehydroepiandrosterone Sulfotransferase: Purification and Characterization of a Recombinant Protein
    • Chang, H.J., Zhou, M., Lin, S.X.: Human Dehydroepiandrosterone Sulfotransferase: Purification and Characterization of a Recombinant Protein, J Steroid Biochem Mol Biol., vol. 77 (2-3), p159 (2001).
    • (2001) J Steroid Biochem Mol Biol. , vol.77 , Issue.2-3 , pp. 159
    • Chang, H.J.1    Zhou, M.2    Lin, S.X.3
  • 10
    • 0033554394 scopus 로고    scopus 로고
    • Effect of Mutation at Valine 61 on the Three-Dimensional Structure, Stability, and Redox Potential of Cytochrome b5
    • Xue, L.L., Wang, Y.H., Xie, Y., Yao, P., Wang, W.H., Qian, W., Huang, Z.X., Wu, J., Xia, Z.X.: Effect of Mutation at Valine 61 on the Three-Dimensional Structure, Stability, and Redox Potential of Cytochrome b5, Biochemistry, vol. 38 (37), p11961 (1999).
    • (1999) Biochemistry , vol.38 , Issue.37 , pp. 11961
    • Xue, L.L.1    Wang, Y.H.2    Xie, Y.3    Yao, P.4    Wang, W.H.5    Qian, W.6    Huang, Z.X.7    Wu, J.8    Xia, Z.X.9
  • 11
    • 0030887028 scopus 로고    scopus 로고
    • Structure and Mechanism of Phosphoenolpyruvate Carboxykinase
    • Matte, A., Tari, L.W., Goldie, H., Delbaere, L.T.: Structure and Mechanism of Phosphoenolpyruvate Carboxykinase, J Biol Chem., vol. 272(13), p8105 (1997).
    • (1997) J Biol Chem. , vol.272 , Issue.13 , pp. 8105
    • Matte, A.1    Tari, L.W.2    Goldie, H.3    Delbaere, L.T.4
  • 12
    • 0031081675 scopus 로고    scopus 로고
    • Purification, Characterization and Conformational Analysis of a Haemorrhagin from the Venom of Agkistrodon Acutus
    • Zhu, Z., Gong, W., Zhu, X., Teng, M., Niu, L: Purification, Characterization and Conformational Analysis of a Haemorrhagin from the Venom of Agkistrodon Acutus, Toxicon, vol. 35 (2), p283 (1997).
    • (1997) Toxicon , vol.35 , Issue.2 , pp. 283
    • Zhu, Z.1    Gong, W.2    Zhu, X.3    Teng, M.4    Niu, L.5
  • 13
    • 85039613239 scopus 로고    scopus 로고
    • Purification and Activation in vitro of MoFe Protein from a nifE Deleted Mutant strain of Azotobacter vinelandii
    • in press
    • Zhao, J.-F., Zhao, Y., Wang Z.-P., Lv Y.-B., Qian, Z.-X., Huang J.-F.: Purification and Activation in vitro of MoFe Protein from a nifE Deleted Mutant strain of Azotobacter vinelandii, Chin. Acta of Botany, in press.
    • Chin. Acta of Botany
    • Zhao, J.-F.1    Zhao, Y.2    Wang, Z.-P.3    Lv, Y.-B.4    Qian, Z.-X.5    Huang, J.-F.6
  • 15
    • 0034984464 scopus 로고    scopus 로고
    • Avian Hemoglobins and Structural Basis of High Affinity for Oxygen: Structure of Bar-headed Goose Aquomet Haemoglobin
    • Liu, X.Z., Li, S.L., Jing, H., Liang, Y.H., Hua, Z.Q., Lu, G.Y.: Avian Hemoglobins and Structural Basis of High Affinity for Oxygen: Structure of Bar-headed Goose Aquomet Haemoglobin, Acta Crystallogr D, Biol Crystallogr., vol. 57 (Pt 6), p775 (2001).
    • (2001) Acta Crystallogr D, Biol Crystallogr. , vol.57 , Issue.PART 6 , pp. 775
    • Liu, X.Z.1    Li, S.L.2    Jing, H.3    Liang, Y.H.4    Hua, Z.Q.5    Lu, G.Y.6
  • 16
    • 20444403817 scopus 로고    scopus 로고
    • The Crystallization and Preliminary Crystallographic Analysis of the Monoclinic Crystal Form of Basic Phospholipase A2 from the Venom of Agkistrodon halys Pallas
    • Niu, X.T., Meng, W.Y., Gui, L.L., Wang, X.Q., Lin, Z.J., Gu, P.Z., Zhu, Y.C.: The Crystallization and Preliminary Crystallographic Analysis of the Monoclinic Crystal Form of Basic Phospholipase A2 from the Venom of Agkistrodon halys Pallas, J. Biochemistry & Biophysics, Sinica, vol. 28(2), p206 (1996).
    • (1996) J. Biochemistry & Biophysics, Sinica , vol.28 , Issue.2 , pp. 206
    • Niu, X.T.1    Meng, W.Y.2    Gui, L.L.3    Wang, X.Q.4    Lin, Z.J.5    Gu, P.Z.6    Zhu, Y.C.7
  • 17
    • 0032284470 scopus 로고    scopus 로고
    • The Pre-experiment on Space Crystallization of Pig Heart Mitochondrial F1-ATPase
    • Li, S.G., Yang S.Z., Du Q., Chen H.L., Lin, Z.H.: The Pre-experiment on Space Crystallization of Pig Heart Mitochondrial F1-ATPase, Space Medicine & Medical Engineering, 11(5), p343-346 (1998).
    • (1998) Space Medicine & Medical Engineering , vol.11 , Issue.5 , pp. 343-346
    • Li, S.G.1    Yang, S.Z.2    Du, Q.3    Chen, H.L.4    Lin, Z.H.5
  • 18
    • 0032208930 scopus 로고    scopus 로고
    • Numerical Studies on the Pre-nucleation Transport in the Liquid/Liquid Diffusion Crystallization of Proteins
    • Gang, H.-X., Bi, R.-C.: Numerical Studies on the Pre-nucleation Transport in the Liquid/Liquid Diffusion Crystallization of Proteins, J. Crystal Growth, vol. 194, p133 (1998).
    • (1998) J. Crystal Growth , vol.194 , pp. 133
    • Gang, H.-X.1    Bi, R.-C.2
  • 19
    • 0033198416 scopus 로고    scopus 로고
    • Crystallization within Agarose Gel in Microgravity Improves the Quality of Thaumatin Crystals
    • Lorber, B., Sauter, C., Robert, M.C., Capelle, B., Giegé, R.: Crystallization within Agarose Gel in Microgravity Improves the Quality of Thaumatin Crystals, Acta Cryst., D55, p1491 (1999).
    • (1999) Acta Cryst. , vol.D55 , pp. 1491
    • Lorber, B.1    Sauter, C.2    Robert, M.C.3    Capelle, B.4    Giegé, R.5
  • 20
    • 0032474989 scopus 로고    scopus 로고
    • Gel Growth of Lysozyme Crystals Studied by Small Angle Neutron Scattering: Case of Agarose Gel, a Nucleation Promotor
    • Vidal, O., Robert, M.C., Boue, F.: Gel Growth of Lysozyme Crystals Studied by Small Angle Neutron Scattering: Case of Agarose Gel, a Nucleation Promotor, J. Crystal Growth vol. 192, p257 (1998).
    • (1998) J. Crystal Growth , vol.192 , pp. 257
    • Vidal, O.1    Robert, M.C.2    Boue, F.3
  • 21
    • 0033290360 scopus 로고    scopus 로고
    • Protein Crystal Growth-Microgravity Aspects
    • Vekilov, P.G.: Protein Crystal Growth-Microgravity Aspects, Adv. Space Res., vol. 24 (10), p1231 (1999).
    • (1999) Adv. Space Res. , vol.24 , Issue.10 , pp. 1231
    • Vekilov, P.G.1
  • 22
    • 0035501928 scopus 로고    scopus 로고
    • Mosaic Spread Analysis of Canadian Advanced Protein Crystallization Experiment on the Russian Space Station
    • Yoon, T.-S., Tetreault, S., Bosshard, H.E., et al.: Mosaic Spread Analysis of Canadian Advanced Protein Crystallization Experiment on the Russian Space Station, Mir, J. Crystal Growth, vol. 232 (1-4), p520 (2001).
    • (2001) Mir, J. Crystal Growth , vol.232 , Issue.1-4 , pp. 520
    • Yoon, T.-S.1    Tetreault, S.2    Bosshard, H.E.3
  • 23
    • 0034477286 scopus 로고    scopus 로고
    • Influence of Microgravity on Protein Crystal Structures
    • Dong, J., Pan, J.-S., Niu, X.-T., Zhou, Y.-C, Bi, R.-C.: Influence of Microgravity on Protein Crystal Structures, Chin. Sci. Bulletin, vol. 45 (11), p1002 (2000).
    • (2000) Chin. Sci. Bulletin , vol.45 , Issue.11 , pp. 1002
    • Dong, J.1    Pan, J.-S.2    Niu, X.-T.3    Zhou, Y.-C.4    Bi, R.-C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.