Crystallization and preliminary X‐ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP. Issue 3 (1st March 2014)

• Record Type: Journal Article
• Authors: Balotra, Sahil; Newman, Janet; French, Nigel G.; Briggs, Lyndall J.; Peat, Thomas S.; Scott, Colin
• Is Part Of: Acta crystallographica. Volume 70:Issue 3(2014:Mar.)
• Page Start: 310
• Page End: 315
• Publication Date: 2014-03-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X13034705
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The allophanate hydrolase from <italic>Pseudomonas</italic> 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 <italic>P</italic>2₁, with unit‐cell parameters <italic>a</italic> = 82.4, <italic>b</italic> = 179.2, <italic>c</italic> = 112.6 Å, β = 106.6°.</p> </abstract>