Dehydration converts DsbG crystal diffraction from low to high resolution

Structure

Volumn 11, Issue 2, 2003, Pages 139-145

  Heras, Begoña ^a   Edeling, Melissa A ^a   Byriel, Karl A ^a   Jones, Alun ^a   Raina, Satish ^b   Martin, Jennifer L ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b UNIVERSITY OF GENEVA MEDICAL SCHOOL   (Switzerland)

Author keywords

Crystal dehydration; Disulfide isomerase; Dsb proteins; X ray diffraction

Indexed keywords

ARTICLE; CONTROLLED STUDY; CRYSTAL; CRYSTALLOGRAPHY; DEHYDRATION; DISULFIDE BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; X RAY DIFFRACTION;

CRYSTALLOGRAPHY, X-RAY; DESICCATION; ESCHERICHIA COLI PROTEINS; GLYCEROL; OXIDOREDUCTASES; PERIPLASMIC PROTEINS; WATER;

EID: 0037318396     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(03)00005-4     Document Type: Article

References (43)

1. Harp J.M., Timm D.E., Bunick G.J. Macromolecular crystal annealing. overcoming increased mosaicity associated with cryocrystallography Acta Crystallogr. D Biol. Crystallogr. 54:1998;622-628.
2. Harp J.M., Hanson B.L., Timm D.E., Bunick G.J. Macromolecular crystal annealing. evaluation of techniques and variables Acta Crystallogr. D Biol. Crystallogr. 55:1999;1329-1334.
3. Schick B., Jurnak F. Crystal growth and crystal improvement strategies. Acta Crystallogr. D Biol. Crystallogr. 50:1994;563-568.
4. Kawashima T., Berthet-Colominas C., Cusack S., Leberman R. Interconversion of crystals of the Escherichia coli EF-Tu.EF-Ts complex between high-and low-diffraction forms. Acta Crystallogr. D Biol. Crystallogr. 52:1996;799-805.
5. Cramer P., Muller C.W. Engineering of diffraction-quality crystals of the NF-κB P52 homodimer:DNA complex. FEBS Lett. 405:1997;373-377.
6. Esnouf R.M., Ren J., Garman E.F., Somers D.O., Ross C.K., Jones E.Y., Stammers D.K., Stuart D.I. Continuous and discontinuous changes in the unit cell of HIV-1 reverse transcriptase crystals on dehydration. Acta Crystallogr. D Biol. Crystallogr. 54:1998;938-953.
7. Tong L., Qian C., Davidson W., Massariol M.-J., Bonneau P.R., Cordingley M.G., Lagacé L. Experiences from the structure determination of human cytomegalovirus protease. Acta Crystallogr. D Biol. Crystallogr. 53:1997;682-690.
8. Yang J.K., Yoon H.J., Ahn H.J., Lee B.I., Cho S.H., Waldo G.S., Park M.S., Suh S.W. Crystallization and preliminary X-ray crystallographic analysis of the Rv2002 gene product from Mycobacterium tuberculosis, a β-ketoacyl carrier protein reductase homologue. Acta Crystallogr. D Biol. Crystallogr. 58:2002;303-305.
9. Kim H.-W., Han B.W., Yoon H.-J., Yang J.K., Lee B.I., Lee H.H., Ahn H.J., Suh S.W. Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Pseudomonas aeruginosa. Acta Crystallogr. D Biol. Crystallogr. 58:2002;1874-1875.
10. Pang S.S., Guddat L.W., Duggleby R.G. Crystallization of the FAD-independent acetolactate synthase of Klebsiella pneumoniae. Acta Crystallogr. D Biol. Crystallogr. 58:2002;1237-1239.
11. Madhusudan B., Kodandapani R., Vijayan M. Protein hydration and water structure. X-ray analysis of a closely packed protein crystal with very low solvent content Acta Crystallogr. D Biol. Crystallogr. 49:1993;234-245.
12. Dobrianov I., Kriminski S., Caylor C.L., Lemay S.G., Kimmer C., Kisselev A., Finkelstein K.D., Thorne R.E. Dynamic response of tetragonal lysozyme crystals to changes in relative humidity. implications for post-growth crystal treatments Acta Crystallogr. D Biol. Crystallogr. 57:2001;61-68.
13. Fu Z.-Q., Du Bois G.C., Song S.P., Harrison R.W., Weber I.T. Improving the diffraction quality of MTCP-1 crystals by post-crystallization soaking. Acta Crystallogr. D Biol. Crystallogr. 55:1999;5-7.
14. Izard T., Sarfaty S., Westphal A., de Kok A., Hol W.G. Improvement of diffraction quality upon rehydration of dehydrated icosahedral Enterococcus faecalis pyruvate dehydrogenase core crystals. Protein Sci. 6:1997;913-915.
15. Haebel P.W., Wichman S., Goldstone D., Metcalf P. Crystallization and initial crystallographic analysis of the disulfide bond isomerase DsbC in complex with the α domain of the electron transporter DsbD. J. Struct. Biol. 136:2001;162-166.
16. Collet J.F., Bardwell J.C. Oxidative protein folding in bacteria. Mol. Microbiol. 44:2002;1-8.
17. Bader M., Muse W., Ballou D.P., Gassner C., Bardwell J.C. Oxidative protein folding is driven by the electron transport system. Cell. 98:1999;217-227.
18. Martin J.L. Thioredoxin - a fold for all reasons. Structure. 15:1995;245-250.
19. Bardwell J.C., McGovern K., Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell. 67:1991;581-589.
20. Bardwell J.C., Lee J.O., Jander G., Martin N., Belin D., Beckwith J. A pathway for disulfide bond formation in vivo. Proc. Natl. Acad. Sci. USA. 90:1993;1038-1042.
21. Guilhot C., Jander G., Martin N.L., Beckwith J. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. Proc. Natl. Acad. Sci. USA. 92:1995;9895-9899.
22. Zapun A., Missiakas D., Raina S., Creighton T.E. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry. 34:1995;5075-5089.
23. Missiakas D., Schwager F., Raina S. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14:1995;3415-3424.
24. Rietsch A., Belin D., Martin N., Beckwith J. An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc. Natl. Acad. Sci. USA. 93:1996;13048-13053.
25. Bessette P.H., Cotto J.J., Gilbert H.F., Georgiou G. In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG. J. Biol. Chem. 274:1999;7784-7792.
26. Goldstone D., Haebel P.W., Katzen F., Bader M.W., Bardwell J.C., Beckwith J., Metcalf P. DsbC activation by the N-terminal domain of DsbD. Proc. Natl. Acad. Sci. USA. 98:2001;9551-9556.
27. Chen J., Song J.L., Zhang S., Wang Y., Cui D.F., Wang C.C. Chaperone activity of DsbC. J. Biol. Chem. 274:1999;19601-19605.
28. Shao F., Bader M.W., Jakob U., Bardwell J.C. DsbG, a protein disulfide isomerase with chaperone activity. J. Biol. Chem. 275:2000;13349-13352.
29. McCarthy A.A., Haebel P.W., Torronen A., Rybin V., Baker E.N., Metcalf P. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. Nat. Struct. Biol. 7:2000;196-199.
30. Garman E. Cool data. quantity AND quality Acta Crystallogr. D. 55:1999;1641-1653.
31. Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
32. Timasheff S.N. Solvent stabilization of protein structure. Methods Mol. Biol. 40:1995;253-269.
33. Frey M. Water structure associated with proteins and its role in crystallisation. Acta Crystallogr. D Biol. Crystallogr. 50:1994;663-666.
34. Perutz, M.F. (1946). The composition and swelling properties of haemoglobin crystals. Trans. Faraday Soc., Volume XLII B, 187-195.
35. Boyes-Watson J., Davidson E., Perutz M.F. An X-ray study of horse methaemoglobin. I. Proc. Roy. Soc. A. 191:1947;83-132.
36. Green D.W., Ingram V.M., Perutz M.F. The structure of haemoglobin IV. Sign determination by the isomorphous replacement method. Proc. Roy. Soc. A. 225:1954;287-307.
37. Huxley H.E., Kendrew J.C. Discontinuous lattice changes in haemoglobin crystals. Acta Crystallogr. D Biol. Crystallogr. 6:1953;76-80.
38. Einstein J.R., Low B.W. Insulin. Some shrinkage stages of sulfate and citrate crystals. Acta Crystallogr. 15:1962;32-34.
39. Salunke D.M., Veerapandian B., Kodandapani R., Vijayan M. Water-mediated transformations in protein crystals. Acta Crystallogr. B Struct. Sci. 41:1985;431-436.
40. Kodandapani R., Suresh C.G., Vijayan M. Crystal structure of low humidity tetragonal lysozyme at 2.1 Å resolution. Variability in hydration shell and its structural consequences. J. Biol. Chem. 265:1990;16126-16131.
41. Kachalova G.S., Morozov V.N., Morozova T.Ya., Myachin E.T., Vagin A.A., Strokopytov B.V., Nekrasov Yu.V. Comparison of structures of dry and wet hen egg-white lysozyme molecule at 1.8 Å resolution. FEBS Lett. 284:1991;91-94.
42. Nagendra H.G., Sukumar N., Vijayan M. Role of water in plasticity, stability, and action of proteins. the crystal structures of lysozyme at very low levels of hydration Proteins. 32:1998;229-240.
43. Edeling M., Guddat L.W., Fabianek R.A., Halliday J.A., Jones A., Thöny-Meyer L., Martin J.L. Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE). Acta Crystallogr. D Biol. Crystallogr. 57:2001;1293-1295.