Crystallization and preliminary X-ray analysis of the controller protein C.Ahdl from Aeromonas hydrophilia


McGeehan, J.E., Streeter, S., Cooper, J.B., Mohammed, F., Fox, G.C. and Kneale, G.G. (2004) Crystallization and preliminary X-ray analysis of the controller protein C.Ahdl from Aeromonas hydrophilia. Acta Crystallographica Section D: Biological Crystallography, 60, (2), 323-325. (doi:10.1107/S0907444903026143).

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Description/Abstract

Single crystals of purified homodimeric controller protein from Aeromonas hydrophilia (C.AhdI) have been grown under several different conditions using vapour diffusion. X-ray diffraction data have been collected using synchrotron radiation from crystals of both the native and a selenomethionine (SeMet) derivative of the protein. The native crystal form belongs to space group P21 and data were collected to a resolution of 2.2 Å. Two crystal forms of the SeMet protein have been obtained and were found to belong to space groups P1 and P21; data have been recorded to 2.0 and 1.7 Å resolution, respectively, for the two crystal forms. Three-wavelength MAD data were collected to 1.7 Å for the SeMet derivative crystal, which is isomorphous with the native P21 crystal.

Item Type: Article
ISSNs: 0907-4449 (print)
Related URLs:
Keywords: aeromonas hydrophilia, dna-binding proteins, dna-modification methylases
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: University Structure - Pre August 2011 > School of Biological Sciences
ePrint ID: 56682
Date Deposited: 06 Aug 2008
Last Modified: 27 Mar 2014 18:39
URI: http://eprints.soton.ac.uk/id/eprint/56682

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