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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt 3):226-31. doi: 10.1107/S1744309109001511. Epub 2009 Feb 12.

Expression, purification and crystallization of class C acid phosphatases from Francisella tularensis and Pasteurella multocida.

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1
Department of Chemistry, University of Missouri-Columbia, 65211, USA.

Abstract

Class C nonspecific acid phosphatases are bacterial enzymes that are secreted across the cytoplasmic membrane and hydrolyze a variety of phosphomonoesters at acidic pH. These enzymes are of interest for the development of improved vaccines and clinical diagnostic methods. In one case, the category A pathogen Francisella tularensis, the class C phosphatase plays a role in bacterial fitness. Here, the cloning, expression, purification and crystallization methods for the class C acid phosphatases from F. tularensis and Pasteurella multocida are reported. Crystals of the F. tularensis enzyme diffracted to 2.0 A resolution and belonged to space group C222(1), with one enzyme molecule in the asymmetric unit. Crystals of the P. multocida enzyme diffracted to 1.85 A resolution and belonged to space group C2, with three molecules in the asymmetric unit. Diffraction patterns from crystals of the P. multocida enzyme exhibited multiple interpenetrating reciprocal-space lattices, indicating epitaxial twinning. Despite this aberrance, autoindexing was robust and the data could be satisfactorily processed to 1.85 A resolution using MOSFLM and SCALA.

PMID:
19255471
PMCID:
PMC2650447
DOI:
10.1107/S1744309109001511
[Indexed for MEDLINE]
Free PMC Article
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