AI Article Synopsis
- Crystals of the hypothetical protein TdcF from E. coli were successfully grown using vapour diffusion methods.
- The protein crystallized in the P2(1)2(1)2 space group, with specific unit-cell dimensions measured at a = 72.67, b = 86.22, c = 62.62 Å.
- Native X-ray data was collected at a resolution of 2.35 Å from a single crystal at 100 K, suggesting the presence of a trimer in the asymmetric unit, confirmed through molecular-replacement with the YjgF trimer structure.
Article 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.
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