| Autor: |
Vévodová J; Department of Chemistry, University of York, Heslington, York YO10 5YW, England., Graham RM, Raux E, Warren MJ, Wilson KS |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2005 Apr 01; Vol. 61 (Pt 4), pp. 442-4. Date of Electronic Publication: 2005 Apr 01. |
| DOI: |
10.1107/S1744309105006731 |
| Abstrakt: |
CobE, a protein implicated in vitamin B12 biosynthesis, from Pseudomonas aeruginosa has been overexpressed in Escherichia coli, purified and crystallized using hanging-drop vapour diffusion. The crystals belong to the primitive orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 31.86, b = 41.07, c = 87.41 A. The diffraction extends to a resolution of 1.9 A. There is one molecule per asymmetric unit and the estimated solvent content is 35%. SeMet-labelled CobE has been prepared and crystallizes under the same conditions as the native protein with diffraction to 1.7 A. The anomalous measurements will be used for phasing. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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