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:
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.
The advent of brain organoid technology has enabled scientists to begin to ask what makes us human. Madeline Lancaster’s group has identified differences in early brain development that can help to explain the increased number of neurons in human brains over other apes.
Rare lipids in our cell membranes act as postcodes to operate regulatory processes such as autophagy and endocytosis. Roger Williams, together with Sean Munro’s and John Brigg’s groups, have shown how the G-proteins Rab1 and Rab5 activate these processes respectively, through conformational changes of kinase VPS34 complexes.
- LMB scientists honoured by Biochemical Society Awards
LMB scientists Sjors Scheres, Maria Marti Solano and alumnus Tanmay Bharat have all been awarded prizes in the 2022 Biochemical Society Awards […]
- 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. […]
- Immortalized Canine Dystrophic Myoblast Cell Lines for Development of Peptide-Conjugated Splice-Switching Oligonucleotides.
Tone, Y., et al.
Nucleic Acid Ther 31(2): 172-181. (9th April 2021)
- Correction to: Cryo-EM structures of tau filaments from Alzheimer's disease with PET ligand APN-1607.
Shi, Y., et al.
Acta Neuropathol [Epub ahead of print]. (8th April 2021)
- XFEL Crystal Structures of Peroxidase Compound II.
Kwon, H., et al.
Angew Chem Int Ed Engl [Epub ahead of print]. (7th April 2021)
- PANDORA-seq expands the repertoire of regulatory small RNAs by overcoming RNA modifications.
Shi, J., et al.
Nat Cell Biol 23(4): 424-436. (5th April 2021)
- Using RELION software within the Scipion framework.
Sharov, G., Morado, DR., Carroni, M., de la Rosa-Trevín, JM.
Acta Crystallogr D Struct Biol 77(Pt 4): 403-410. (1st April 2021)
- Structure of the complete, membrane-assembled COPII coat reveals a complex interaction network.
Hutchings, J., Stancheva, VG., Brown, NR., Cheung, ACM., Miller, EA., Zanetti, G.
Nat Commun 12(1): 2034. (1st April 2021)
- Structural basis for conformational equilibrium of the catalytic spliceosome.
Wilkinson, ME., Fica, SM., Galej, WP., Nagai, K.
Mol Cell 81(7): 1439-1452.e9. (1st April 2021)
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