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°.
Original language | English |
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Pages (from-to) | 310-315 |
Number of pages | 6 |
Journal | Acta Crystallographica Section F:Structural Biology Communications |
Volume | 70 |
Issue number | 3 |
DOIs | |
Publication status | Published - Mar 2014 |
Externally published | Yes |