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

Mayuko Toyoda, Keiji Jitsumori, Bunzo Mikami, Lawrence P. Wackett, Tatsuo Kurihara, Nobuyoshi Esaki

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

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 VM value was 2.2 Å3 Da-1, suggesting that the crystal contains one enzyme subunit in the asymmetric unit.

Original languageEnglish (US)
Pages (from-to)801-804
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number7
DOIs
StatePublished - 2010

Keywords

  • L-azetidine-2-carboxylate hydrolase
  • Pseudomonas sp. strain A2C

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