Lisa Strittmatter, PhD student in the LMB’s Structural Studies Division, explores a recent talk given at the LMB by Professor Sir John Meurig Thomas, and the light it sheds on the key scientists involved in the origins of molecular biology. More…
Finding the founding fathers of molecular biology – a blog post by LMB PhD student, Lisa Strittmatter
Brain research in the third dimension
Madeline Lancaster, cell biologist at the MRC Laboratory of Molecular Biology in Cambridge, has developed a technique allowing her to create mini brains from cell cultures. These incredible organoids, no larger than the eraser at the end of a pencil, serve as a model for Madeline’s research into early human brain development and are enabling Madeline and her team to tackle the age-old question: what is it that distinguishes us as humans? More…
LMB scientist wins ‘Best Technology’ prize in the 2017 Biomaker Challenge
The LMB’s Wolfgang Schmied, in collaboration with Stéphanie Polderdijk from the Cambridge Institute for Medical Research, won ‘Best Technology’ prize in the 2017 Biomaker Challenge for developing a low-cost chromatography system for protein purification. The Challenge aims to show the value of open, low-cost and DIY technologies as convening points for interactions between biologists and engineers. More…
BBC: Daytime wounds ‘heal more quickly’
A new study led by John O’Neill and Ned Hoyle shows how bodyclocks in skin cells influence wound healing. More…
Using cryo-EM to solve the structure of a protein complex critical for gene expression
Lori Passmore and her group have used electron cryo-microscopy to solve the structure of CPF, a protein complex critical for gene expression. Understanding the structure and function of intact CPF, and how it is assembled, has been a central question in the field of gene expression for decades. [A Log-in or subscription may be required to view this article from the host site: https://www.drugtargetreview.com/news/27088/cryo-electron-microscopy-cpf/]
PINK1 caught on the brink of phosphorylation
Scientists have caught a rare view of an unusual kinase poised to phosphorylate its substrate. Led by David Komander, MRC Laboratory of Molecular Biology in Cambridge, England, U.K., the researchers reported the crystal structure of the kinase PINK1 bound to ubiquitin in the October 30 Nature. “We captured a pre-catalytic state, a snapshot of PINK1 holding ubiquitin before the phosphate group jumps on,” said first author Alexander Schubert. More…