Newcastle University MX Structural Biology Laboratory
Welcome
Hello, you’ve reached the Newcastle MX Structural Biology Laboratory, part of the Newcastle University Biosciences Institute (NUBI), University of Newcastle. The NSBL was founded in 2003, but in the last ~6 months we have undergone some restructure and there are now 3 research institutes withint the facutly of medical sciences. Two groups in NUBI, Paula Salgado and Bert van den Berg, concentrate their research activities on important questions in microbial lifestyle:
How do bacteria build the protective wall that protects the cell?
How do bacteria co-ordinate cell division and cell growth?
How do bacteria protect themselves from the host immune system during infection?
How do bacteria traffic molecules into and out of the cell?
Two groups Martin Noble and Jane Endicott in Newcastle University Translational and Clinical Research Institute (NUTCRI) are interested in understanding the progression through the eukaryotic cell cycle at the molecular level, and in exploiting that knowledge to produce new chemical probes and potential leads for drug discovery.
Jon Marles-Wright from the Newcastle University School of Natural and Environmental Sciences is using structural biology to answer questions relating to the function of bacterial compartmentalization systems and their rational design as platforms for biotechnology and synthetic biology.
Arnaud Baslefrom the Newcastle University Biosciences Institute is the MX X-ray facilities manager. While supporting NSBL Arnaud aslo collaborate with non-structural biology labs.
Methanobactin from Methylocystis hirsuta CSC1 (A) and M. strain M (B). Carbon atoms are represented in light or dark gray, oxygen in red, nitrogen in blue and sulphur in yellow. Hydrogen bonds are represented in black or red dash lines.
Structure of a HTCS periplasmic domain monomer colour ramped blue to red from the N-terminus. A transmembrane helix is predicted after the C-terminus of the construct used for crystallisation. Native data were collected on beamline I02 and Se-met SAD data collected on beamline I04. Ligand data were collected on beamline I24.
Crystal of of SlpA complex constituted by the Low (LMW) and High Molecular Weight (HMW) proteins, formed after processing of precursor SlpA.Crystal of of SlpA complex constituted by the Low (LMW) and High Molecular Weight (HMW) proteins, formed after processing of precursor SlpA.