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Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP.
- Source :
-
Acta Crystallographica: Section F, Structural Biology Communications . Mar2014, Vol. 70 Issue 3, p310-315. 6p. - Publication Year :
- 2014
-
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°. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 2053230X
- Volume :
- 70
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F, Structural Biology Communications
- Publication Type :
- Academic Journal
- Accession number :
- 94777816
- Full Text :
- https://doi.org/10.1107/S2053230X13034705