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Acta Crystallogr F Struct Biol Commun. 2014 Mar;70(Pt 3):310-5. doi: 10.1107/S2053230X13034705. Epub 2014 Feb 19.

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

Author information

1
Ecosystem Sciences, CSIRO, GPO Box 1700, Canberra, ACT 2601, Australia.
2
Materials, Science and Engineering, CSIRO, 343 Royal Parade, Parkville, VIC 3052, Australia.

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°.

KEYWORDS:

AtzF; Pseudomonas sp. strain ADP; allphanate hydrolase; amidase domain

PMID:
24598916
PMCID:
PMC3944691
DOI:
10.1107/S2053230X13034705
[Indexed for MEDLINE]
Free PMC Article

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