| Autor: |
Ellis J; Department of Biochemistry, University of Leicester, Leicester LE1 7RH, England., Campopiano DJ, Izard T |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 1999 May; Vol. 55 (Pt 5), pp. 1086-8. |
| DOI: |
10.1107/s0907444999003029 |
| Abstrakt: |
Chloramphenicol 3-O-phosphotransferase (CPT) from Streptomyces venezuelae ISP5230, a novel chloramphenicol-inactivating kinase, has been overexpressed and purified using Escherichia coli as the heterologous host. Crystals of CPT in complex with its substrate chloramphenicol (Cm) were obtained which were suitable for X-ray diffraction. The crystals belong to the cubic space group I4132 with unit-cell dimension a = 200.0 A. The initial CPT crystals diffracted to 3.5 A and the diffraction was improved significantly upon adding acetonitrile and Cm to the crystallization drop. The CPT-Cm crystals diffract to at least 2.8 A resolution. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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