Crystallization and preliminary X-ray analysis of L-azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C

Autor: Toyoda, Mayuko, Jitsumori, Keiji, Mikami, Bunzo, Wackett, Lawrence P, Kurihara, Tatsuo, Esaki, Nobuyoshi
Jazyk: angličtina
Rok vydání: 2010
Předmět:
Zdroj: Acta crystallographica. Section F, Structural biology and crystallization communications. 66(Pt 7):801-804
ISSN: 1744-3091
Popis: L-Azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C catalyzes a ring-opening reaction that detoxifies L-azetidine-2-carboxylate, an analogue of L-proline. Recombinant L-azetidine-2-carboxylate hydrolase was overexpressed, purified and crystallized using polyethylene glycol and magnesium acetate as precipitants. The needle-shaped crystal belonged to space group P2(1), with unit-cell parameters a = 35.6, b = 63.6, c = 54.7 A, beta = 105.5 degrees . The crystal diffracted to a resolution of 1.38 A. The calculated V(M) value was 2.2 A(3) Da(-1), suggesting that the crystal contains one enzyme subunit in the asymmetric unit.
Databáze: OpenAIRE