Oxford Protein Production Facility UK
The Oxford Protein Production Facility UK is a structural proteomics facility in the Division of Structural Biology of the Department of Medicine, Oxford University, funded by the Medical Research Council and Biotechnology and Biological Sciences Research Council as a National Resource Centre for protein production and crystallization.
The OPPF-UK aims to promote and facilitate high throughput structural biology for the UK academic community. It is the first stage in a structural proteomics programme for the UK and represents an essential stepping stone toward the practical exploitation of the wealth of information coming from the human genome sequencing projects.
The OPPF-UK is located in the Research Complex at Harwell, adjacent to the Diamond Light Source.
©2010 Medical Research Council
We offer parallel vector construction and expression screening and access to high-throughput crystallization using 100nl sitting drops. Please go to the Services tab for details. To apply, please register on our website and then complete a proposal form available under the Services tab. The OPPF-UK is open to all UK academic groups and the use of our facilities is "free at the point of access".
For information about transnational access to this facility, please go to the P-CUBE website.
Lobley CM, Aller P, Douangamath A, Reddivari Y, Bumann M, Bird LE, Nettleship JE, Brandao-Neto J, Owens RJ, O'Toole PW, Walsh MA. Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1427-33.
Yates LA, Lumb CN, Brahme NN, Zalyte R, Bird LE, De Colibus L, Owens RJ, Calderwood DA, Sansom MS, Gilbert RJ. Structural and functional characterization of the kindlin-1 pleckstrin homology domain. J Biol Chem. 2012 Dec 21;287(52):43246-61.
Porta C, Xu X, Loureiro S, Paramasivam S, Ren J, Al-Khalil T, Burman A, Jackson T, Belsham GJ, Curry S, Lomonossoff GP, Parida S, Paton D, Li Y, Wilsden G, Ferris N, Owens R, Kotecha A, Fry E, Stuart DI, Charleston B, Jones IM. Efficient production of foot-and-mouth disease virus empty capsids in insect cells following down regulation of 3C protease activity. J Virol Methods. 2012 Nov 19.
Berry JL, Phelan MM, Collins RF, Adomavicius T, Tønjum T, Frye SA, Bird L, Owens R, Ford RC, Lian LY, Derrick JP. Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis. PLoS Pathog. 2012 Sep;8(9):e1002923.
Sainsbury S, Ren J, Saunders NJ, Stuart DI, Owens RJ. Structure of the regulatory domain of the LysR family regulator NMB2055 (MetR-like protein) from Neisseria meningitidis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):730-7.
Research at the Oxford Protein Production Facility is enabled primarily by grants from the Medical Research Council with additional support from the Biotechnology and Biological Sciences Research Council.
