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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°.