Crystallization and preliminary X‐ray analysis of dihydrodipicolinate synthase from Clostridium botulinum in the presence of its substrate pyruvate

Crystallization and preliminary X‐ray analysis of dihydrodipicolinate synthase from Clostridium... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystallization and preliminary X‐ray analysis of dihydrodipicolinate synthase from Clostridium botulinum in the presence of its substrate pyruvate

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Publisher
Wiley
Copyright
International Union of Crystallography, 2009
ISSN
1744-3091
eISSN
1744-3091
D.O.I.
10.1107/S1744309108039018
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Acta Crystallographica Section FWiley

Published: Mar 1, 2009

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