UK MAD BEAMLINE AT ESRF
Lead Research Organisation:
Medical Research Council
Department Name: UNLISTED
Abstract
Macromolecular crystallography is the most powerful method available to biologists to determine the precise three-dimensional arrangement of atoms within proteins and other complex biological molecules. By tuning the wavelength of X-rays such that they interact strongly with certain atoms within the molecule researchers can more easily unravel the complete structure. This method is called MAD and this grant asks for funds to provide open access to all UK researchers to one of the top MAD beamlines in Europe. The output of BM14 will be several hundred new structures some of which are likely to be of great biomedical importance.
Technical Summary
BM14 is a dedicated macromolecular crystallography beamline at the ESRF that is currently being operated by the UK Research Councils as a Collaborative Research group (CRG). The beamliine was designed specifically for anomalous diffraction experiments, in particular, MAD and SAD, which are the methods of choice for the de novo structure determination of biological macromolecules. It provides the UK crystallographic community with open and rapid access to a third generation synchrotron tuneable beamline through a paperless, web-based peer-reviewed beamline application system.
BM14 is arguably the most stable and successful MAD beamline in Europe, being cited in some 100 papers in 2004 alone. This proposal requests funds to enable BM14 to continue this provision for the UK community to mesh with the start-up of operations at the new UK synchrotron, DIAMOND.
BM14 is arguably the most stable and successful MAD beamline in Europe, being cited in some 100 papers in 2004 alone. This proposal requests funds to enable BM14 to continue this provision for the UK community to mesh with the start-up of operations at the new UK synchrotron, DIAMOND.
Publications
Albesa-Jové D
(2010)
Four distinct structural domains in Clostridium difficile toxin B visualized using SAXS.
in Journal of molecular biology
Alfieri A
(2008)
Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase.
in Proceedings of the National Academy of Sciences of the United States of America
Andersson CS
(2009)
A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold.
in Proceedings of the National Academy of Sciences of the United States of America
Aricescu AR
(2008)
Receptor protein tyrosine phosphatase micro: measuring where to stick.
in Biochemical Society transactions
Ash MR
(2010)
Conserved beta-hairpin recognition by the GYF domains of Smy2 and GIGYF2 in mRNA surveillance and vesicular transport complexes.
in Structure (London, England : 1993)
Bagnéris C
(2008)
Crystal structure of a vFlip-IKKgamma complex: insights into viral activation of the IKK signalosome.
in Molecular cell
Bahar MW
(2008)
Structure and function of A41, a vaccinia virus chemokine binding protein.
in PLoS pathogens
Bandeiras T
(2010)
Purification, crystallization and X-ray crystallographic analysis of Archaeoglobus fulgidus neelaredoxin
in Acta Crystallographica Section F Structural Biology and Crystallization Communications
Bhatt TK
(2010)
Ligand-bound structures provide atomic snapshots for the catalytic mechanism of D-amino acid deacylase.
in The Journal of biological chemistry
Bird LE
(2010)
Novel structural features in two ZHX homeodomains derived from a systematic study of single and multiple domains.
in BMC structural biology
| Description | BM14 |
| Geographic Reach | Asia |
| Policy Influence Type | Influenced training of practitioners or researchers |
| Description | Automation of protein crytallography |
| Organisation | European Molecular Biology Laboratory |
| Department | European Molecular Biology Laboratory Grenoble outstation |
| Country | France |
| Sector | Academic/University |
| PI Contribution | Harware and software development |
| Collaborator Contribution | improvements to beamline design. Design comercialised by EMBL, recognising MRC imput. Now implemented at several sitesContibution to development of ispyb database implemented at ESRF and Diamond. |
| Impact | publications and hardware and software installed at ESRF and Diamond |
| Start Year | 2007 |
| Description | Automation of protein crytallography |
| Organisation | European Synchrotron Radiation Facility |
| Country | France |
| Sector | Charity/Non Profit |
| PI Contribution | Harware and software development |
| Collaborator Contribution | improvements to beamline design. Design comercialised by EMBL, recognising MRC imput. Now implemented at several sitesContibution to development of ispyb database implemented at ESRF and Diamond. |
| Impact | publications and hardware and software installed at ESRF and Diamond |
| Start Year | 2007 |