On day 287 of #LMB365 we see an image of a bee’s leg taken by a pupil at Stapleford Primary School and submitted for the LMB’s 2019 Science Image Award. We’re now starting to recruit nearby primary schools for next year’s competition https://www2.mrc-lmb.cam.ac.uk/microscopes4schools/award.php
LMB 365 – Day 287
LMB 365 – Day 286
Day 286 of #LMB365 shows the developing Cambridge Biomedical Campus taken by Paul Margiotta from the nearby Nine Wells nature reserve. The LMB’s plant towers can be seen between the Anne McLaren Facility (left) and the Royal Papworth Hospital (blue) and Abcam (right).
LMB 365 – Day 285
The production of purified macromolecular samples can be very challenging. Subsequently it is hard to schedule exactly when the final sample preparation will be obtained. Samples produced at the LMB can be screened anytime for crystallisation because crystallisation trays filled up with with a broad variety of initial screens (LMB screens) are made readily available to users of the crystallisation facility. A fully automated pipetting system prepares the LMB screens, as seen here on day 285 of #LMB365.
Fast, simple, accessible and affordable: The future of cryo-EM
Is it possible to improve imaging of purified biological specimens in electron cryo-microscopy (cryo-EM) while also reducing its cost? The latest proof-of-principle paper from Chris Russo’s group says yes, and indicates that the answer lies in reducing the electron energy in the cryo-EM from the current standard of 300 or 200 kiloelectron volts (keV) to 100 keV. Recent measurements of radiation damage to biological specimens by high-energy electrons have shown that at lower energies there is an increased amount of information available per unit damage. The authors of the paper foresee that future cryo-microscopes designed for ultimate single-particle resolution will be designed to maximise this information. This will then make true atomic resolution (~1 Å) more accessible and affordable.
Structural insights into control of cell growth by nutrient availability
Control of cell division is crucially important, as unregulated cell division is a hallmark of cancer. mTORC1 protein kinase is an ancient enzyme complex and master regulator of growth and metabolism that integrates signals relating to nutrient availability, energy, and growth factors. Activation of mTORC1 is driven by proteins called Rags that sense nutrient abundance. However, some cancer-causing mutations make Rag proteins active even in the absence of nutrients and drive cells to divide when they shouldn’t. Roger Williams’ group, in the LMB’s PNAC Division, has now shown how active Rags bind to mTORC1 and how a cancer-associated mutation can make a Rag protein continuously active.
LMB 365 – Day 284
The LMB postgraduate students are a truly international and diverse community. Every year 20-30 new graduates from the UK and all over the world join the LMB PhD programme. This photo for day 284 of #LMB365 shows this year’s intake on their first day in the Lab.