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 |
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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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