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

摘要

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 P21, with unit-cell parameters a = 35.6, b = 63.6, c = 54.7 Å, β = 105.5°. The crystal diffracted to a resolution of 1.38 Å. The calculated V M value was 2.2 ų Da⁻¹, suggesting that the crystal contains one enzyme subunit in the asymmetric unit.