ArticleActa crystallographica. Section F, Structural biology and crystallization communications2006
Crystallization and preliminary crystallographic studies of the Pasteurella multocida toxin catalytic domain.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin.The Journal of biological chemistry · 2010Article
- Crystal structures reveal a thiol protease-like catalytic triad in the C-terminal region of Pasteurella multocida toxin.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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5 authors.
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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 A 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 A, beta = 105.5 degrees, and are likely to contain one C-PMT (726 residues) per asymmetric unit.
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