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

The amidase domain of the allophanate hydrolase AtzF from Pseudomonas sp. strain ADP has been crystallized and preliminary X-ray diffraction data have been collected. 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 P2{sub 1}, with unit-cell parameters a = 82.4, b = 179.2, c = 112.6 Å, β = 106.6°.
Authors:
 [1] ;  [2] ; ;  [1] ;  [2] ;  [1]
  1. CSIRO, GPO Box 1700, Canberra, ACT 2601 (Australia)
  2. CSIRO, 343 Royal Parade, Parkville, VIC 3052 (Australia)
Publication Date:
OSTI Identifier:
22375680
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta crystallographica. Section F, Structural biology communications; Journal Volume: 70; Journal Issue: Pt 3; Other Information: PMCID: PMC3944691; PMID: 24598916; PUBLISHER-ID: no5038; OAI: oai:pubmedcentral.nih.gov:3944691; Copyright (c) Balotra et al. 2014; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; RESOLUTION; SPACE GROUPS; STRAINS; X-RAY DIFFRACTION