In this paper, the crystallization and preliminary X‐ray diffraction analysis to near‐atomic resolution of DHDPS from Clostridium botulinum crystallized in the presence of its substrate pyruvate are presented. The enzyme crystallized in a number of forms using a variety of PEG precipitants, with the best crystal diffracting to 1.2 Å resolution and belonging to space group C2, in contrast to the unbound form, which had trigonal symmetry. The unit‐cell parameters were a = 143.4, b = 54.8, c = 94.3 Å, β = 126.3°. The crystal volume per protein weight (VM) was 2.3 Å3 Da−1 (based on the presence of two monomers in the asymmetric unit), with an estimated solvent content of 46%. The high‐resolution structure of the pyruvate‐bound form of C. botulinum DHDPS will provide insight into the function and stability of this essential bacterial enzyme.
Acta Crystallographica Section F – Wiley
Published: Mar 1, 2009
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