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

Sahil Balotra, Janet Newman, Nigel G. French, Lyndall J. Briggs, Thomas S. Peat, Colin Scott*

*Corresponding author for this work

Research output: Contribution to journalArticle

8 Citations (Scopus)
2 Downloads (Pure)

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 languageEnglish
Pages (from-to)310-315
Number of pages6
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
Issue number3
DOIs
Publication statusPublished - 2014
Externally publishedYes

Bibliographical note

Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

Keywords

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

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