Space-grown protein crystals are more useful for structure determination

Annals of the New York Academy of Sciences

Volumn 974, Issue , 2002, Pages 598-609

  Ng, Joseph D ^a  

^a UNIVERSITY OF ALABAMA IN HUNTSVILLE   (United States)

Author keywords

Aspartyl tRNA synthetase; Crystal quality; Crystallization microgravity; Mosaicity; Pea lectin; Protein; Thaumatin

Indexed keywords

ASPARTATE TRANSFER RNA LIGASE; LECTIN; PROTEIN; THAUMATIN;

AB INITIO CALCULATION; ACCURACY; CONFERENCE PAPER; CRYSTALLIZATION; DENSITY; GRAVITY; MICROGRAVITY; MOLECULAR MODEL; MOSAICISM; NONHUMAN; SPACE; STRUCTURE ANALYSIS; THERMUS THERMOPHILUS; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

PISUM; PISUM SATIVUM; THAUMATOCOCCUS DANIELLII; THERMUS; THERMUS THERMOPHILUS;

EID: 0037024603     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2002.tb05934.x     Document Type: Conference Paper

References (46)

1. Littke, W. & C. John. 1984. Protein single crystal growth under microgravity. Science 225: 203-204.
2. DeLucas, L.J., K.M. Moore & M.M. Long. 1999. Protein crystal growth and the International Space Station. Gravit. Space Biol. Bull. 12: 39-45.
3. Moore, K.M., M.M. Long & L.J. DeLucas. 1999. Space Technology and Applications Int. Forum. M.S. EI-Genk, Ed. 458: 217-224. American Institute of Physics.
4. McPherson, A. 1999. Crystallization of Biological Macromolecules. Cold Spring Harbor Press, Cold Spring Harbor, New York.
5. Couzin, J. 1998. Negative review galls space crystallographers. Science 281: 497-498.
6. McPherson, A. 1997. Recent advances in the microgravity crystallization of biological macromolecules. Trends Biotech. 15: 197-200.
7. Kundrot, C.E., R.A. Judge, M.L. Pusey & E. Snell. 2000. Microgravity and macromolecular crystallography. Cryst. Growth Design 1: 87-99.
8. McPherson, A. 1996. Macromolecular crystal growth in microgravity. Crystallogr. Rev. 6: 157-305.
9. Ng, J.D., B. Lorber, R. Giegé, et al. 1997. Comparative analysis of thaumatin crystals grown on earth and in microgravity. Acta Crystallogr. D53: 724-733.
10. Carter, D.C., K. Lim, J.X. Ho, et al. 1999. Lower dimer impurity incorporation may result in higher perfection of HEWL crystals grown in microgravity. A case study. J. Cryst. Growth 196: 623-637.
11. Chayen, N.E. & J.R. Helliwell. 1999. Space-grown crystals may prove their worth. Nature 398: 20.
12. Declercq, J.-P., et al. 1999. A crystal of a typical EF-hand protein grown under microgravity diffracts X-rays beyond 0.9 Å resolution. J. Cryst. Growth 196: 595-601.
13. Lorber, B., C. Sauter, M.-C. Robert, et al. 1999. Crystallization within agarose gel in microgravity improves the quality of thaumatin crystals. Acta Crystallogr. D55: 1491-1494.
14. DeLucas, L.J., et al. 2000. Space Technology and Application International Forum. CP504. 488.
15. Ng, J.D., C. Sauter, B. Lorber, et al. 2002. Comparative analysis of space- and Earth-grown crystals of an aminoacyl-tRNA synthetase: Space-grown crystals are more useful for structure determination. Acta Crystallogr. D58: 645-652.
16. Vaney, M.C., M, Maignan, M. Riès-Kautt & A. Ducruix. 1996. High-resolution structure (1.33Å) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from Spacehab-01 mission. Acta Crystallogr. D52: 505-517.
17. Dong, J., T.J. Boggon, N.E. Chayen, et al. 1999. Bound-solvent structures for microgravity-, ground control-, gel-, and microbatch-grown hen egg-white lysozyme crystals at 1.8 Å resolution. Acta Crystallogr. D55: 745-752.
18. Otálora, F., M.L. Novella, J.A. Gavira, et al. 2001. Experimental evidence for the stability of the depletion zone around a growing protein crystal under microgravity. Acta Cryst. D57: 412-417.
19. Sauter, C., F. Otálora, J.A. Gavira, et al. 2001. Structure of tetragonal hen egg-white lysozyme at 0.94 Å from crystals grown by the counter-diffusion method. Acta Crystallogr. D57: 1119-1126.
20. Borgstahll, G.E.O., A. Vahedi-Faridi, H. Bellamy & E.H. Snell. 2001. A test of macromolecular crystallization in microgravity: large, well ordered insulin crystals. Acta Crystallogr. D57: 1204-1207.
21. DeLucas, L.J., C.D. Smith, H.W. Smith, et al. 1989. Protein crystal growth in microgravity. Science 246: 651-654.
22. Helliwell, J.R. 1988. Protein crystal perfection and the nature of radiation damage. J. Cryst. Growth 90: 259-272.
23. Weisgerber, S. & J.R. Helliwell. 1993. Chicken egg-white lysozyme crystal grown in microgravity and on Earth for a comparison on their respective perfection. Joint CCP4 & ESF-EACBM Newsletter on Protein Crystallography 29: 10-13.
24. Snell, E., H.S. Weisgerber, J.R. Helliwell, et al. 1995. Improvements in lysozyme protein crystal perfection through microgravity growth. Acta Crystallogr. D51: 1099-1102.
25. Ferrer, J.L., J. Hirschler, M. Roth & J. Fontecilla-Camps. 1996. ESRF Newsletter 27.
26. Lorber, B., C. Sauter, J.D. Ng, et al. 1999. Characterization of protein and virus crystals by quasi-planar wave X-ray topography: A comparison between crystals grown in solution and in agarose gel. J. Cryst. Growth 204: 357-368.
27. van der Wel, H., T.C. van Soest & E.C. Royers. 1975. Crystallization and crystal data of thaumatin I, a sweet-tasting protein from Thaumatococcus daniellii benth. FEBS Lett. 56: 316-317.
28. McPherson, A. & J. Weickmann. 1990. X-ray analysis of new crystal forms of the sweet protein thaumatin. J. Biomol. Struct. Dyn. 5: 1053-1060.
29. Bosch, R., P. Lautenschlager, L. Potthast & J. Stapelmann. 1992. Experimental equipment for protein crystallization in microgravity facilities. J. Cryst. Growth 122: 310-316.
30. Becker, H.D., J. Reinbolt, R. Kreutzer, et al. 1997. Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus. Structural and biochemical properties of the two enzymes. Biochemistry 36: 8785-8797.
31. Poterszman, A., P. Plateau, D. Moras, et al. 1993. Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases. FEBS Lett. 325: 183-186.
32. Delarue, M., A. Poterszman, S. Nikonov, et al. 1994. Crystal structure of a prokaryotic aspartyl-tRNA synthetase. EMBO J. 13: 3219-3229.
33. Ng, J.D., B. Lorber, J. Witz, et al. 1996. Crystal growth of macromolecules from precipitation: evidence for Ostwald ripening. J. Cryst. Growth 168: 50-62.
34. Phillips, D.C. 1966. Advances in Protein Crystallography, Advances in Structure Research by Diffraction Methods. 75-140. F. Wiweg, Brauschweig.
35. Drenth, J. 1995. Principles of Protein X-ray Crystallography. 153-182. Springer-Verlag, New York.
36. Rossman, M.G. 1972. The Molecular Replacement Method. Gordon and Breach, London.
37. Dauter, Z., M. Dauter, E. de La Fortelle, et al. 1999. Can anomalous signal of sulfur become a tool for solving protein crystal structures? J. Mol. Biol. 289: 83-92.
38. 2+-regulated photoprotein obelin at 1.7 Å resolution determined directly form its sulfur substructure, Protein Sci. 9: 2085-2093.
39. Wang, B.C. 1985. Resolution of phase ambiguity in macromolecular crystallography. Meth. Enzymol. 115: 90-112.
40. Gavira, J.A., D. Toh, J. Lopéz-Jaramillo, et al. 2002. Ab initio crystallographic structure determination of insulin from protein to electron density without crystal handling. Acta Crystallogr. D58: 1147-1154.
41. Otwinowski, Z. & W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Meth. Enzymol. 276: 307-326.
42. Brünger, A., A.T. Adams, P. D. Clore, et al. 1998. Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D54: 905-921.
43. Jones, T.A., J.-Y. Zou, S.W. Cowan & M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47: 110-119.
44. Delarue, M., A. Poterszman, S. Nikonov, et al. 1994. Crystal structure of a prokaryotic aspartyl-tRNA synthetase. EMBO J. 13: 3219-3229.
45. McPherson, A. 1982. Preparation and Analysis of Protien Cystals. John Wiley & Sons, New York.
46. Prasthofer, T., S.R. Phillips, F.L. Suddath & J.A. Engler. 1989. Design, expression and crystallization of recombinant lectin from the garden pea (Pisum sativum). J. Biol. Chem. 264: 6793-6796.