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

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

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

Author(s) -

Balotra Sahil,

Newman Janet,

French Nigel G.,

Briggs Lyndall J.,

Peat Thomas S.,

Scott Colin

Publication year - 2014

Publication title -

acta crystallographica section f

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.572

H-Index - 37

ISSN - 2053-230X

DOI - 10.1107/s2053230x13034705

Subject(s) - amidase , resolution (logic) , hydrolase , pseudomonas , strain (injury) , crystallization , chemistry , microbiology and biotechnology , stereochemistry , enzyme , biochemistry , biology , bacteria , organic chemistry , computer science , anatomy , genetics , artificial intelligence

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 P 2 1 , with unit‐cell parameters a = 82.4, b = 179.2, c = 112.6 Å, β = 106.6°.

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