Abstract
Microgravity in space offers an ideal environment for growing protein crystals, where there is an absence of density-driven convection and sedimentation. Using domestic apparatus of protein crystalizetion, two space experiments of protein crystal growth have been carried out on the Chinese re-entry satellite, and good-quality hen egg-white lysozyme crystals were obtained. To study the effect of microgravity on the prorein crystal structure, three structures of lysozyme crystals grown in gravity and microgravity were determined at high resolution.
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Blake, C. C. F., Fenn, R. H., North, A. C. T. et at., Structure of lysozyme,Nature (London), 1962, 196: 1173.
Diamond, A., Real-space refinement of the structure of hen egg-white lysozyme,J. Mol. Biol., 1974, 82: 371.
Hodsdon, J. M. Brown, G. M., Sieker, L. C. et al., Refinement of triclinic lysozyme: I. Fourier and leat-squares methods,Acta Cryst., 1990, B46: 54.
Harata, K., X-ray structure of a monoclinic form of hen egg-white lysozyme crystallized at 313K. Comparison of two independent molecules,Acta Cryst., 1994, D50: 250.
Bi, R. C., Gui, L. L., Shi, K. et al., Protein crystal growth in microgravity.Science in China, Ser. B, 1994, 37(10): 1185.
Wang, Y. P., Pan, J. S., Bi, R. C. et al., The second space experiment of protein crystallization with domestic facilities,Science in China. Ser. C, 1996, 39(5): 458.
Dong, J., Kin, Q., Chu, N. M. et al., Structural studies on space-grown crystals of lysozyme,Chinese Science Bulletin, 1995, 40(8): 672.
Vaney, M. C., Maignan, S., Ries-Kautt, M. et al., High-resolution structure (1.33 Å) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from Space Hab01 mission,Acta Cryst., 1996, D52: 505.
Brunger, A. T., Kuriyan, J., Karplus, M., Crystallographic R factor refinement by molecular dynamics,Science, 1987, 235: 458.
Laskowski, R. A., MacArthur, M. W., Moss, D. S., et al., Procheck: a program to check the steremhemical quality of protein structures,J. Appl. Crpt., 1993, 26: 283.
Luzzati, P. V., Traitement statisque des erreurs dans la determination des structures cristallines,Acta Cryst., 1952. 5: 802.
Kundrot, C. E., Richards, F. M., Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres,J. Mol. Biol., 1987, 193: 157.
Kurinov, I. V., Harrison, R. W., The influence of temperature on lysozyme crystals structure and dynamics of protein and water,Acta Cryst., 1995, D5l:98.
Jeffrey, G. A., Maluszynska, H., A swey of hydrogen bond geometries in the crystal structures of amino acids.lnt, J. Biol. Macromol., 1982, 4: 173.
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Project supported by the National Program of Space Application.
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Dong, J., Wang, Y., Han, Q. et al. Structural study on hen egg-white lysozyme crystals grown in gravity and microgravity. Sci. China Ser. C.-Life Sci. 41, 238–244 (1998). https://doi.org/10.1007/BF02895097
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DOI: https://doi.org/10.1007/BF02895097