People

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 www.raddo.se.

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 January 2017

Research assistant

Joshua Dickerson — Improving RADDOSE-3D

I am making improvements to the group’s dose calculation software, RADDOSE-3D. My main focus is on improving the accuracy of the calculated dose by implementing a fluorescent X-ray escape model and improving and extending the current photoelectron escape model.

  • Joined the group in November 2017





Page Last Updated: 24/01/2018 by Helena Taberman
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