Crystallization and preliminary X-ray analysis of the controller protein C.Ahdl from Aeromonas hydrophilia
Crystallization and preliminary X-ray analysis of the controller protein C.Ahdl from Aeromonas hydrophilia
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.
aeromonas hydrophilia, dna-binding proteins, dna-modification methylases
323-325
McGeehan, J.E.
c209c216-ac04-4e38-a780-900d53122186
Streeter, S.
58a2493a-5fc3-4a95-8adc-49b2bc06cd13
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Mohammed, F.
e6dd5a98-bea5-484a-873a-da499c034594
Fox, G.C.
8d2bf25c-f7b1-44bb-8775-ecb86a682339
Kneale, G.G.
5942b32e-f877-4efa-b39f-66f09a79f911
1 February 2004
McGeehan, J.E.
c209c216-ac04-4e38-a780-900d53122186
Streeter, S.
58a2493a-5fc3-4a95-8adc-49b2bc06cd13
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Mohammed, F.
e6dd5a98-bea5-484a-873a-da499c034594
Fox, G.C.
8d2bf25c-f7b1-44bb-8775-ecb86a682339
Kneale, G.G.
5942b32e-f877-4efa-b39f-66f09a79f911
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), .
(doi:10.1107/S0907444903026143).
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.
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Published date: 1 February 2004
Keywords:
aeromonas hydrophilia, dna-binding proteins, dna-modification methylases
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Local EPrints ID: 56682
URI: http://eprints.soton.ac.uk/id/eprint/56682
ISSN: 0907-4449
PURE UUID: 30fed545-dda0-4ce0-b1b8-74f0c03e462b
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Date deposited: 06 Aug 2008
Last modified: 15 Mar 2024 11:03
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Contributors
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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