LMB 365 – Day 237

On day 237 of #LMB365 is a model of the structure of the enzyme, F1-ATPase. The structure was first published one this day in 1994 in a landmark paper in Nature. F1-ATPase is the catalytic component of ATP synthase, the enzyme responsible for the synthesis of ATP in living cells. The gamma subunit (blue) is believed to rotate within the three alpha (red) and three beta (yellow) subunits during catalysis. For his work in solving this structure John Walker shared the 1997 Nobel Prize in Chemistry. Jan Pieter Abrahams, Andrew G. W. Leslie, René Lutter; John E. Walker. Structure at 2.8 angstrom resolution of F1-ATPase from bovine heart mitochondria. Nature 370: 621-628, 1994

Day 236 of #LMB365,taken by Neil Grant in the LMB’s Visual Aids team, shows the geometric patterns and reflections that can be seen when exploring the exterior of the LMB building on a sunny day.

On day 235 of #LMB365 PhD student Ross Hill celebrates with fellow students and postdocs the publication of his first paper from his PhD. The culmination of 3½ years of work and the ultimate accolade: to see your work reaching the scientific community. Worth a toast! Read more at https://t.co/G8ylgimczZ?amp=1

Amoebae and some cancer cells can feed by swallowing large gulps of their surrounding medium. An amoeba can drink nearly its own volume in an hour – an amazing feat if scaled to humans. This process is known as macropinocytosis, and has been studied by Rob Kay’s group in the Cell Biology Division. Day 234 of #LMB365 shows cells forming cups from their plasma membrane. These are shaped around a patch of the lipid PIP3 (orange), surrounded by a necklace of the SCAR/WAVE protein (green) that guides formation of the walls of the cup

Scientists rely on antibodies, proteins produced by the mammalian immune system, which are able to identify very specific molecules. Day 233 of #LMB365 shows Saša Šviković, from Julian Sale’s lab in the PNAC division, purifying antibodies from litres of cells grown in the lab by passing them through a column able to trap them. This approach has been used extensively ever since César Milstein and Georges Koehler (both PNAC alumni) developed technology to produce monoclonal antibodies, for which they won the Nobel Prize in 1984. The antibodies will be used to investigate how cells respond to various obstacles encountered during the duplication of DNA

The LMB’s NMR facility is home to five of the LMB’s seven NMR spectrometers, and is also currently hosting a spectrometer for our future neighbours AstraZeneca while their building is being completed. This photograph for day 232 of #LMB365 shows our highest strength, 800 MHz, magnet which is typically used for studying larger protein systems or when the most sensitivity is required. Liquid helium maintains the magnetic coils of the spectrometer at a chilly 1.9 kelvin: removing all electrical resistance, which allows the charge to remain indefinitely without a power source. Many people do not realise that we can’t simply switch off our magnets once energised.