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The Bacillus subtilis YphC gene encodes an essential GTPase thought to be involved in ribosome binding and whose protein product may represent a target for the development of a novel antibacterial agent. Sequence analysis reveals that YphC belongs to the EngA family of GTPases, which uniquely contain two adjacent GTP‐binding domains. Crystals of a selenomethionine‐incorporated YphC–GDP complex have been grown using the hanging‐drop vapour‐diffusion method and polyethylene glycol as a precipitating agent. The crystals belong to space group P212121, with unit‐cell parameters a = 62.71, b = 65.05, c = 110.61 Å, and have one molecule in the asymmetric unit. Data sets at three different wavelengths were collected on a single crystal to 2.5 Å resolution at the Daresbury SRS in order to solve the structure by MAD. Ultimately, analysis of YphC in complex with GDP may allow a greater understanding of the EngA family of essential GTPases.
Acta Crystallographica Section F – Wiley
Published: May 1, 2006
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