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- Title
Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP.
- Authors
Balotra, Sahil; Newman, Janet; French, Nigel G.; Briggs, Lyndall J.; Peat, Thomas S.; Scott, Colin
- 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°.
- Subjects
HYDROLASES regulation; PSEUDOMONAS syringae; IMMUNOGLOBULIN E; CELL receptors; CRYSTALLIZATION
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2014, Vol 70, Issue 3, p310
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X13034705