Lori Passmore and Chris Russo from the LMB’s Structural Studies Division have discovered how to modify the new material graphene using low-energy hydrogen plasmas, to allow it to bind proteins. This discovery makes it suitable for use in electron microscopy to solve protein structures.
Graphene, which was only discovered in 2004, is a two-dimensional carbon sheet that is one of the strongest and thinnest materials known.
Graphene: stronger than steel and now suitable for biological electron microscopy
New technique identifies protein production in specific cells at specific times
Research undertaken by Jason Chin’s group, in the LMB’s Centre for Chemical and Synthetic Biology (CCSB), part of the Protein and Nucleic Acid Chemistry Division, has successfully developed a novel and versatile technique to identify proteins produced in a particular set of cells at a particular time.
Individual sets of cells in the body of an animal are specialised to do different things.
Shedding light on how mRNA molecules navigate to their destination within the cell
Harish Chandra Soundararajan and Simon Bullock from the LMB’s Cell Biology Division have created a new technique for studying how dynein motors move individual mRNA molecules along microtubules, which has provided unique insights into cellular transport systems.
In order for a cell to function, its constituents have to be sorted to different locations. In many cases, this is achieved by an active intracellular transport system.
Breakthrough in structural biology reveals mitochondrial ribosome structure
The bringing together of several independent lines of research by members of the LMB’s Structural Studies Division has led to the determination of the atomic structure of the yeast mitochondrial ribosome. The work took advantage of recent developments in electron microscopy (EM), brought about by a decade of work at the LMB to develop better EM detectors.
Coupling of transcription termination and mRNA processing
Work carried out by Lori Passmore’s group in the LMB’s Structural Studies Division, in collaboration with Patrick Cramer’s group in Munich, has revealed how transcription termination and mRNA processing by Cleavage and Polyadenylation Factor (CPF) are coupled via dephosphorylation of the C-terminal domain of RNA Polymerase II by CPF.
Genes code for proteins – the ‘doing-molecules’ in cells.