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. 2005 Aug 1;61(Pt 8):759-61.
doi: 10.1107/S1744309105021093. Epub 2005 Jul 30.

Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus

Kenichiro Suzuki  1 , Sohei Ito, Akiko Shimizu-Ibuka, Hiroshi Sakai
Affiliations

Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus

Kenichiro Suzuki et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

Pyruvate kinase (PK) from a moderate thermophile, Bacillus stearothermophilus (BstPK), is an allosteric enzyme activated by AMP and ribose 5-phosphate but not by fructose 1,6-bisphosphate (FBP). However, almost all other PKs are activated by FBP. The wild-type and W416F/V435W mutant BstPKs were crystallized by the hanging-drop vapour-diffusion method. However, they were unsuitable for structural analysis because their data sets exhibited low completeness. A crystal suitable for structural analysis was obtained using C9S/C268S enzyme. The crystal belonged to space group P6(2)22, with unit-cell parameters a = b = 145.97, c = 118.03 A.

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Figures

Figure 1
Figure 1
BstPK crystals. (a) Wild type, (b) W416F/V435W, (c) C9S/C268S.
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