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).
Full text not available from this repository.
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.
|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
|Date Deposited:||06 Aug 2008|
|Last Modified:||06 Aug 2015 02:46|
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
Actions (login required)