Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP

Sahil Balotra, Janet Newman, Nigel G. French, Lyndall J. Briggs, Thomas S. Peat, Colin Scott

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

The allophanate hydrolase from Pseudomonas sp. strain ADP was expressed and purified, and a tryptic digest fragment was subsequently identified, expressed and purified. This 50 kDa construct retained amidase activity and was crystallized. The crystals diffracted to 2.5 Å resolution and adopted space group P21, with unit-cell parameters a = 82.4, b = 179.2, c = 112.6 Å, β = 106.6°.

Original languageEnglish
Pages (from-to)310-315
Number of pages6
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
Issue number3
DOIs
Publication statusPublished - Mar 2014
Externally publishedYes

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