Laboratory of Molecular Biophysics Laboratory Journal 2001 Dr. E. F. Garman

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Elspeth Garman

Radiation Damage Studies of Cryo-Cooled Protein Crystals and Mutational Investigation of Neuraminidases.

Introduction.

This year we have expanded the scope of our investigations into radiation damage in cryocooled protein crystals, and we have started a new research program in which we are producing active site mutants of Salmonella typhimurium LT2 sialidase with the long term aim of elucidating the enzyme mechanism.

The radiation damage studies have comprised two parts: a) the systematic study of the use of scavengers in cryo-cooled (100K) crystals as a possible way of mitigating radiation damage inflicted by second and third generation synchrotrons, and b) the investigation of on-line monitoring of unit cell expansion as a radiation damage metric.

We have continued to use the Proton Microprobe here in the Department of Materials to analyse both liquid and crystalline protein samples. We have expended effort in trying to improve the method for reliable quantitative detection of trace elements in liquid samples at low concentration, and in understanding the limitations in terms of protein size and concentration. This work is still ongoing.

An interest is maintained in the development of further anti-influenza drugs and the wider issue of planning for pandemic influenza, a subject addressed very recently in Science (Laver and Garman, Science Perspectives, 2001; 293, 1776-1777).

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