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Crystallization and preliminary X-ray analysis of the E. coli hypothetical protein TdcF.

作者信息

Burman Julia D, Stevenson Clare E M, Hauton Katherine A, Sawers Gary, Lawson David M

机构信息

Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, England.

出版信息

Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1076-8. doi: 10.1107/s0907444903007017. Epub 2003 May 23.

DOI:10.1107/s0907444903007017
PMID:12777779
Abstract

Crystals of the hypothetical protein TdcF (subunit MW = 14 007) from Escherichia coli were grown by vapour diffusion. The protein crystallizes in space group P2(1)2(1)2, with unit-cell parameters a = 72.67, b = 86.22, c = 62.62 A. Native data to a resolution of 2.35 A were collected from a single crystal at 100 K on a rotating-anode X-ray generator. Preliminary analysis of these data indicated that the asymmetric unit corresponded to a trimer, which was supported by a convincing molecular-replacement solution using the YjgF trimer as the probe structure.

摘要

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