In line with government instructions, members of the LMB are working from home where possible. The LMB buildings remain open for research and work that cannot be conducted from home. The LMB COVID-19 risk assessment has been updated and measures are in place to manage the risk from infection including strict social distancing measures in all areas of the building and maintaining high standards of both personal and environmental hygiene, including wearing face masks in all communal spaces and multi-occupancy lab areas.
All meetings will be held via video or teleconferencing. Travel for work is not permitted, nor are visitors to any LMB building unless essential (prior permission required). Please use email as the preferred means of contacting members of LMB.
COVID-19 research remains active at LMB, with over 12 separate strands of research into various aspects of the SARS-CoV-2 virus underway:
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
TRIM21 is both enzyme and substrate when creating a signal to degrade bound viruses and proteins
The intracellular immune receptor TRIM21 detects antibody-bound viruses inside our cells and targets them for destruction by creation of a polyubiquitin signal. David Neuhaus’ group, with Leo James’, has shown that TRIM21 is both the enzyme and recipient of the ubiquitination.
Packaging molecular motors for delivery
The airways in our lungs are kept clear of mucus by the rhythmic beating motion of slender cellular extensions called cilia, driven by dynein motors. Andrew Carter’s group, has discovered a novel protein that packages these molecular motors for delivery into the cilia.
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Latest News
Linda Amos (1943 – 2021)Linda Amos, former Group Leader in the LMB’s Structural Studies Division, died on Sunday 21st February 2021. Linda was an excellent electron microscopist, at the forefront of image analysis and reconstruction. […]
“A journey of small steps” – celebrating Women in Science at the LMBFor the International Day of Women and Girls in Science, we’ve asked a few of our researchers to tell us how and why they ended up in careers in science. […]
Latest Publications
- Publisher Correction: The receptor DNGR-1 signals for phagosomal rupture to promote cross-presentation of dead-cell-associated antigens.
Canton, J., et al.
Nat Immunol 22(3): 391. (28th February 2021) - Controlled Ligand Exchange Between Ruthenium Organometallic Cofactor Precursors and a Naïve Protein Scaffold Generates Artificial Metalloenzymes Catalysing Transfer Hydrogenation.
Biggs, G., et al.
Angew Chem Int Ed Engl [Epub ahead of print]. (22nd February 2021) - RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination.
Kiss, L., Clift, D., Renner, N., Neuhaus, D., James, LC.
Nat Commun 12(1): 1220. (22nd February 2021) - Mutational and biophysical robustness in a pre-stabilized monobody.
Chandler, PG., et al.
J Biol Chem : 100447 [Epub ahead of print]. (19th February 2021) - Structure of the SARS-CoV-2 RNA-dependent RNA polymerase in the presence of favipiravir-RTP.
Naydenova, K., et al.
Proc Natl Acad Sci U S A 118(7). (16th February 2021) - Generation and long-term culture of advanced cerebral organoids for studying later stages of neural development.
Giandomenico, SL., Sutcliffe, M., Lancaster, MA.
Nat Protoc 16(2): 579-602. (16th February 2021) - Rethinking organoid technology through bioengineering.
Garreta, E., et al.
Nat Mater 20(2): 145-155. (16th February 2021)
See more Publications