The University of Southampton
University of Southampton Institutional Repository

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

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.

Full text not available from this repository.

More information

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

Identifiers

Local EPrints ID: 56682
URI: http://eprints.soton.ac.uk/id/eprint/56682
ISSN: 0907-4449
PURE UUID: 30fed545-dda0-4ce0-b1b8-74f0c03e462b

Catalogue record

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

Export record

Altmetrics

Contributors

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

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×