Completed Cells, Biochemistry & Physiology Chemistry

UK mad beamline at esrf

In plain English

AI plain-English summary

A dedicated X-ray beamline in Grenoble, France, will give UK scientists open access to a technique that reveals the atomic structure of proteins. Proteins control nearly every process in the body, from digesting food to fighting infection. To understand how a protein works—or why it malfunctions in disease—researchers need to know the exact position of every atom in its three-dimensional shape. Macromolecular crystallography is the most powerful way to do this, and the MAD (multiple-wavelength anomalous diffraction) method sharpens the picture by tuning X-rays to interact strongly with specific atoms. Currently, UK researchers lack guaranteed access to a top-tier MAD beamline. This grant funds open access to BM14, one of Europe’s best, for the entire UK research community. The beamline is expected to produce several hundred new protein structures. Some will be of direct biomedical importance, revealing targets for drug design or showing how pathogens evade the immune system. Others will advance fundamental understanding of how life works at the molecular level—knowledge that, like past discoveries in structural biology, may underpin future diagnostics, therapies, or synthetic biology tools.

View original technical description
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.

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Researchers

Andrew Leslie (Co-Investigator)David Stuart (Principal Investigator)Guy Dodson (Co-Investigator)Louise Johnson (Co-Investigator)Martin Walsh (Co-Investigator)Neil William Isaacs (Co-Investigator)Simon Phillips (Co-Investigator)

Related Research

Grants with similar aims, by meaning.

Provision of the MAD/XAFS facility for the UK structural biology community
Exploiting XMaS Studies of Highly Correlated Electron Systems, Real Surfaces and Biomaterials
KB mirror project for XMaS
X-ray Diffraction Equipment for Macromolecular Crystallography at York
An advanced cryoEM instrument for the University of Cambridge

Original classification

Research Grant

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