Crystallization and preliminary X-ray diffraction analysis of P30, the transmembrane domain of pertactin, an autotransporter from Bordetella pertussis

Zhu, Y.S., Black, I., Roszak, A.W. and Isaacs, N.W. (2007) Crystallization and preliminary X-ray diffraction analysis of P30, the transmembrane domain of pertactin, an autotransporter from Bordetella pertussis. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 63(7), pp. 593-595. (doi: 10.1107/S1744309107028308)

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Abstract

P30, the 32 kDa transmembrane C-terminal domain of pertactin from Bordetella pertussis, is supposed to form a β-barrel inserted into the outer membrane for the translocation of the passenger domain. P30 was cloned and expressed in inclusion bodies in Escherichia coli. After refolding and purification, the protein was crystallized using the sitting-drop vapour-diffusion method at 292 K. The crystals diffract to a resolution limit of 3.5 Å using synchrotron radiation and belong to the hexagonal space group P6<sub>1</sub>22, with unit-cell parameters a = b = 123.27, c = 134.43 Å.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Isaacs, Professor Neil and Roszak, Dr Aleksander
Authors: Zhu, Y.S., Black, I., Roszak, A.W., and Isaacs, N.W.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
Publisher:Wiley-Blackwell Publishing, Inc.
ISSN:1744-3091
ISSN (Online):1744-3091
Published Online:15 June 2007

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