Department of Biochemistry University of Oxford Department of Biochemistry
University of Oxford
South Parks Road
Oxford OX1 3QU

Tel: +44 (0)1865 613200
Fax: +44 (0)1865 613201
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Group Head

Prof. Elspeth Garman 
My group are interested in the development and optimisation of data collection techniques for structural biology, and in particular for macromolecular crystallography (MX). My background is in Physics, so we tend to apply thinking born of physics to our research. After a year teaching in a Secondary School in Swaziland, Southern Africa , I obtained a B.Sc. in Physics at Durham University and then a Doctorate in Experimental Nuclear Physics at Oxford University in 1980. After working as a Research Officer for 7 years in the Nuclear Physics Department in Oxford, I moved to the Laboratory of Molecular Biophysics in 1987 to look after their newly acquired electronic multi-wire X-ray detector. Since then, I have worked on a variety of problems, and among them has been optimising, understanding and disseminating cryo-crystallographic techniques, and on the physics and chemistry of radiation damage in MX. The group’s latest work is to enable 3-D modelling of the dose absorbed by a protein crystal for any beam conditions and a variety of data collection strategies. This can be found at

More about Elspeth Garman

Postdoctoral fellows

Helena Taberman — 

I obtained my BSc and MSc in Chemistry continuing to PhD in Structural biology at the University of Eastern Finland. With a grant from the Finnish Cultural Foundation to work on ‘overcoming challenges of radiation damage in macromolecular complexes at the atomic level’ I will carry out systematic studies on radiation damage to protein, DNA, protein/DNA and protein/RNA crystals during structure determination by X-ray diffraction at cryo- and room temperatures. The new electron density loss pipeline, RIDL, will be used to calculate per-atom metrics to quantify the sensitivity to specific damage. Secondly, the newly established metric, Bdamage, will be used to search for incorrect metal assignments in the PDB followed by measuring some of these proteins using the microPIXE method to unambiguously identify the metals. The results will be then used to analyse if the re-identification of the metal affects the assumed function of the chosen proteins. The third aim of the project is to further improve RADDOSE-3D, which allows the radiation dose distribution during a diffraction experiment to be calculated with both time and space resolution.

  • Joined the group in February 2017

PhD students

Katharina Jungnickel — Crystallisation of Membrane Transporters

As part of the NanoMem Network ( funded by the European Commission Framework Seven Programme my work is mainly focussed on membrane protein structural biology using novel tools such as X-ray free electron lasers (XFEL). Together with Molecular Dimensions Ltd. and supervision by Prof. Elspeth Garman and Dr. Simon Newstead I work on crystallisation of membrane transporters. I aim to understand the difficulties of structure determination of this class of protein towards development of crystallisation screens and the usage of new techniques in structure determination gaining high resolution data of membrane proteins.

  • Joined the group in September 2013


Charlie Bury — Investigation of X-ray induced radiation damage in proteins, nucleic acids, and their complexes

Significant progress has been made over recent years in understanding how radiation damage mechanisms affect crystalline protein structure determination in macromolecular X-ray crystallography (MX) experiments conducted at 100 K. Despite an active field studying the radiation chemistry of nucleic acids interacting with ionising radiation, few MX investigations exist on ‘specific' damage manifestations (chemical/conformational changes) for crystalline DNA/RNA. Our systematic damage analyses on nucleoprotein case studies have indicated that nucleic acids are intrinsically less radiation-sensitive than protein in both protein -DNA and -RNA systems, at the doses typically accumulated in cryocooled data collection at 3rd generation synchrotrons. In conjunction with these investigations I have additionally been developing an automated tool for objectively detecting and quantifying radiation-induced electron density changes on a per-atom basis, as a function of dose. This approach is widely applicable to the systematic investigation of any single crystal MX damage (or time-resolved) data series. 

  • Joined the group in October​ 2014



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