• Photo of the new LMB building opened in 2012

Applications for the LMB PhD programme are now open. Deadline 5 December 2023.

About Us

The MRC Laboratory of Molecular Biology (LMB) is a research institute dedicated to the understanding of important biological processes at the levels of atoms, molecules, cells and organisms. In doing so, we provide knowledge needed to solve key problems in human health.

Our scientists tackle fundamental, often difficult and long-term research problems. The LMB has made revolutionary contributions to science, such as pioneering X-ray crystallography and electron cryo-microscopy (cryo-EM) to determine protein structures, the sequencing of DNA and the development of monoclonal antibodies. Twelve Nobel Prizes have been awarded for work carried out by LMB scientists.

The LMB also promotes the application and exploitation of our research findings, both by collaboration with existing companies and the founding of new ones, helping to advance medical research and the translation and application of knowledge.

The LMB provides an unsurpassed environment for both young and established researchers, with state-of-the-art facilities and a unique scientific culture. The LMB has always been very diverse, with a truly international outlook. We currently employ men and women from over 50 countries, and LMB alumni work in research organisations across the world.

Insight on Research

New method to untangle the contribution of signalling pathways involved in asymmetric cell division

Graphics illustrating how engineering cortical polarity of the Par-complex in normally unpolarized mammalian cells induces key features of asymmetric cell division, spindle orientation and central spindle asymmetry.

Emmanuel Derivery’s group, in the LMB’s Cell Biology Division, has developed a method to directly untangle the contribution of any signalling pathway involved in asymmetric cell division.

First Cryo-EM structures of homomeric GluA1 AMPA glutamate receptor reveals functional roles for N-terminal domains

Electron cryo-microscopy structures of GluA1 AMPA receptors from Ingo Greger’s group in the LMB’s Neurobiology Division reveals that previously unseen structural flexibility of N-terminal domains is crucial for regulating the open-close speed of ion channel gates and recruiting the receptor into synapses.

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