The Division of Structural Biology (STRUBI) is part of the Nuffield Department of Clinical Medicine (NDM) at the University of Oxford. STRUBI is also part of the Wellcome Trust Centre for Human Genetics. The Division includes the Oxford Protein Production Facility (OPPF) and the Oxford Particle Imaging Centre (OPIC).
STRUBI is situated in the Old Road Campus in the Headington area of Oxford. The Division applies the techniques of structural biology, particularly macromolecular crystallography and electron microscopy, to the study of biomedically important processes. The research interests of the Division include the structural study of viral proteins and intercellular recognition. The work of the laboratory is supported by many sources, but principally the MRC, Cancer Research UK, the BBSRC, the Royal Society, the EU FP6 & FP7 and the Wellcome Trust.
The OPPF
is an MRC-funded project to develop methods and automation for high-throughput structural
proteomics studies of medically important targets. It is particularly focused on protein
production, purification and crystal growth. The OPPF has recently been relocated in the new Research Complex at Harwell, adjacent to the Diamond Light Source to establish the OPPF-UK. Funded by the MRC and BBSRC, the OPPF-UK will be a National Resource Centre for protein production and crystallization.
The OPIC is located in the Henry Wellcome Building for Particle Imaging.
This Wellcome Trust-funded facility allows scientists to study macromolecular complexes, such as human and
animal viruses, in their native cellular environment using a range of structural and biophysical tools.
The facility houses state-of-the-art laboratories at ACDP Cat 3 and DEFRA 4 levels of containment.
allowing study of viruses that are important to human health worldwide, such as HIV and Dengue virus.
The Division of Structural Biology is a
leading player in efforts to coordinate European structural biology. The Division has a five-member team dedicated
to working with the senior academics in the Division to foster international collaboration and help to realize
the goal of integrated large-scale structural biology resources across Europe. These resources would grant access
to all European researchers to allow them to contribute to world-leading research.
For details of the projects in which STRUBI is involved see the Europe tab.
The SPINE2-Complexes EU FP7 project special edition of the Journal of Structural Biology (2011) vol 175/2 is now available as an open access publication!
The Division of Structural Biology (STRUBI) is a research centre of excellence for the study of the molecular and structural basis of biology. Students in STRUBI study a wide range of problems from a structural and mechanistic perspective using a range of structural biology methods including X-ray Crystallography, cryo-electron microscopy, NMR and other biophysical and biochemical methods. Students benefit from our multidisciplinary application of these techniques and from access to state of the art research facilities and equipment. We have a strong history of collaboration where students take advantage of expertise from multiple laboratories to explore novel biological problems. Admission to STRUBI is solely based on excellence: doctoral students have joined the Division after undergraduate studies in subjects ranging from clinical medicine to biochemistry, chemistry and physics. Currently, more than half of our students are from outside the UK, creating a truly international atmosphere.
For details of the projects available please look under the Studentships tab.

Jan 12: Mechanism of Herpex Simplex Virus 1 transport along neurons.
Researchers in the Division of Structural Biology have used electron tomography to analyze the three-dimensional structure of HSV1 particles during anterograde axonal transport. Their data support the 'separate model' for HSV1 egress: that progeny herpes viruses are being transported along axons as subassemblies and not as complete virions within transport vesicles. Read more

Dec 11: New role for perforin in endocytosis.
The human protein perforin is central to 'immune surveillance' whereby white blood cells patrol the body. These 'natural killer' cells use perforin to deliver a signal to virally infected and potentially cancerous cells, causing them to initiate a suicidal response. Researchers in the Division of Structural Biology studying perforin have discovered that in addition to forming pores in cell membranes, the protein can cause a unique form of 'endocytosis' (cell eating) whereby the suicidal signal is taken inside target cells without damaging the outer cell membrane. Read more
To find more news items, look under the News tab.









