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Crystallization and preliminary X-ray analysis of the E. coli hypothetical protein TdcF
Julia D Burman1, Clare E M Stevenson, Katherine A Hauton
1Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, England.
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.