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

Journal Article · Wed Feb 19 00:00:00 EST 2014 · Acta crystallographica. Section F, Structural biology communications

DOI:https://doi.org/10.1107/S2053230X13034705· OSTI ID:22375680

Balotra, Sahil ^[1]; Newman, Janet ^[2]; French, Nigel G.; Briggs, Lyndall J. ^[1]; Peat, Thomas S. ^[2]; Scott, Colin ^[1]

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1. CSIRO, GPO Box 1700, Canberra, ACT 2601 (Australia)
2. CSIRO, 343 Royal Parade, Parkville, VIC 3052 (Australia)

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°.

• OSTI ID: 22375680
• Journal Information: Acta crystallographica. Section F, Structural biology communications, Vol. 70, 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); ISSN 2053-230X
• Country of Publication: United States
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
RESOLUTION
SPACE GROUPS
STRAINS
X-RAY DIFFRACTION