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

Acta crystallographica. Section F, Structural biology and crystallization communications

PubMedID: 16511150

Suzuki K, Ito S, Shimizu-Ibuka A, Sakai H. Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005;61(Pt 8):759-61.
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.