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

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, ? = 106.6°.

SUBMITTER: Balotra S 

PROVIDER: S-EPMC3944691 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature

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

Balotra Sahil S   Newman Janet J   French Nigel G NG   Briggs Lyndall J LJ   Peat Thomas S TS   Scott Colin C  

Acta crystallographica. Section F, Structural biology communications 20140219 Pt 3

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°. ...[more]

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