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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Yuan, Fang Lou, Zhiyong Li, Xiaofeng Chen, Yu Wai Bell, John I. Rao, Zihe Gao, George F. |
| Description | Country affiliation: United kingdom Author Affiliation: Yuan F ( Nuffield Department of Clinical Medicine, John Radcliffe Hospital, Oxford University, Oxford OX3 9DU, England.) |
| Abstract | Domain III of the West Nile virus envelope protein, the putative receptor-binding domain, is a major virion-surface determinant for virulence. This protein was reported to be intrinsically unstable and has defied previous crystallization attempts. It has now been purified from inclusion bodies by protein refolding and was crystallized using the hanging-drop vapour-diffusion method at 291 K. The crystals belong to space group P222(1), with unit-cell parameters a = 52.6, b = 59.7, c = 95.0 A. A complete data set was collected to 2.8 A at 100 K with Cu Kalpha X-rays from a rotating-anode generator. |
| File Format | HTM / HTML |
| ISSN | 2053230X |
| e-ISSN | 17443091 |
| Journal | Acta Crystallographica Section F Structural Biology and Crystallization Communications |
| Issue Number | Pt 4 |
| Volume Number | 61 |
| Language | English |
| Publisher | Wiley |
| Publisher Date | 2005-04-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | Open |
| Subject Keyword | Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Viral Envelope Proteins Chemistry West Nile Virus Binding Sites Crystallization Inclusion Bodies, Viral Protein Folding Protein Structure, Tertiary Volatilization X-ray Diffraction Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics |
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