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Crystallization and preliminary crystallographic studies of the Pasteurella multocida toxin catalytic domain

Crystallization and preliminary crystallographic studies of the Pasteurella multocida toxin... The C‐terminal catalytic domain of Pasteurella multocida toxin, which is the virulence factor of the organism in P. multocida, has been expressed, purified and subsequently crystallized using the sitting‐drop vapour‐diffusion technique. Native diffraction data to 1.9 Å resolution were obtained at the BL44XU beamline of SPring‐8 from a flash‐frozen crystal at 100 K. The crystals belong to space group C2, with unit‐cell parameters a = 111.0, b = 150.4, c = 77.1 Å, β = 105.5°, and are likely to contain one C‐PMT (726 residues) per asymmetric unit. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystallization and preliminary crystallographic studies of the Pasteurella multocida toxin catalytic domain

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References (29)

Publisher
Wiley
Copyright
Copyright © 2006 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309106030375
pmid
16946476
Publisher site
See Article on Publisher Site

Abstract

The C‐terminal catalytic domain of Pasteurella multocida toxin, which is the virulence factor of the organism in P. multocida, has been expressed, purified and subsequently crystallized using the sitting‐drop vapour‐diffusion technique. Native diffraction data to 1.9 Å resolution were obtained at the BL44XU beamline of SPring‐8 from a flash‐frozen crystal at 100 K. The crystals belong to space group C2, with unit‐cell parameters a = 111.0, b = 150.4, c = 77.1 Å, β = 105.5°, and are likely to contain one C‐PMT (726 residues) per asymmetric unit.

Journal

Acta Crystallographica Section FWiley

Published: Sep 1, 2006

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