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.
Enzymes are proteins that accelerate the conversion of substrate molecules into product molecules. Many enzymes accelerate reactions through formation of chemical bonds to their substrates, but the complexes formed this way are difficult to characterise, as they are intrinsically short-lived. In a…
Researchers in Jason Chin’s group in the LMB’s PNAC Division have for the first time engineered and optimised a ‘stapled’ ribosome that can act as a cell-based factory for synthetic protein polymer synthesis. We are familiar with polymers in everyday life, from…
- LMB raises over £1300 for Prostate Cancer UK
LMB staff have raised over £1300 for Prostate Cancer UK at the annual charity Christmas […]
- Songs fill the atrium at the LMB musical evening
After the success of the inaugural event last year, the LMB held its second musical […]
- Jan Löwe talks with the Cambridge Independent about leading the LMB and the next frontier for the laboratory
- Stable research funding drives Britain’s ‘Nobel factory’ – The Financial Times looks into the LMB’s formula for scientific success
- Trapping biosynthetic acyl-enzyme intermediates with encoded 2,3-diaminopropionic acid.
Huguenin-Dezot, N., et al.
Nature [Epub ahead of print]. (12th December 2018)
- Trivalent RING Assembly on Retroviral Capsids Activates TRIM5 Ubiquitination and Innate Immune Signaling.
Fletcher, AJ., Vaysburd, M., Maslen, S., Zeng, J., Skehel, JM., Towers, GJ., James, LC.
Cell Host Microbe 24(6): 761-775.e6. (12th December 2018)
- Structure and architecture of immature and mature murine leukemia virus capsids.
Qu, K., et al.
Proc. Natl. Acad. Sci. U.S.A. 115(50): E11751-E11760. (11th December 2018)
- Hexameric assembly of the AAA+ protein McrB is necessary for GTPase activity.
Nirwan, N., et al.
Nucleic Acids Res. [Epub ahead of print]. (6th December 2018)
- The split protein phosphatase system.
Biochem. J. 475(23): 3707-3723. (6th December 2018)
- Controlling orthogonal ribosome subunit interactions enables evolution of new function.
Schmied, WH., Tnimov, Z., Uttamapinant, C., Rae, CD., Fried, SD., Chin, JW.
Nature [Epub ahead of print]. (5th December 2018)
- SUMOylation of Periplakin is critical for efficient re-organization of Keratin filament network.
Gujrati, M., Mittal, R., Ekal, L., Mishra, RK.
Mol. Biol. Cell : mbcE18040244 [Epub ahead of print]. (5th December 2018)
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