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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), pp. 323-325. (doi:10.1107/S0907444903026143).

Record type: Article


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.

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Published date: 1 February 2004
Keywords: aeromonas hydrophilia, dna-binding proteins, dna-modification methylases


Local EPrints ID: 56682
ISSN: 0907-4449
PURE UUID: 30fed545-dda0-4ce0-b1b8-74f0c03e462b

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Date deposited: 06 Aug 2008
Last modified: 17 Jul 2017 14:30

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Author: J.E. McGeehan
Author: S. Streeter
Author: J.B. Cooper
Author: F. Mohammed
Author: G.C. Fox
Author: G.G. Kneale

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