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John Innes Centre

MP Scientist Pairing Scheme

November 2008

A John Innes Centre scientist has spent a week in Westminster shadowing MP Ian Gibson, as part of a Royal Society scheme that aims to bring parliamentarians and scientists together to understand how scientific knowledge can better inform Government decision making.  

Dr Mark Banfield, a Royal Society University Research Fellow, visited Westminster for a week in November.  He attended Prime Minister’s Questions, a House of Lords debate concerning whether patients who have privately paid for so-called ‘top-up’ drugs should still receive free NHS treatment, and attended select committee meetings, as well as shadowing Dr Gibson, to get a feel for the day-to-day life of an MP.

"My week in Westminster was very interesting. Sitting in on the Department of Innovation, Universities, Science and Skills select committee meetings was particularly informative. I feel I have a better understanding of how science is communicated in Parliament," says Mark.  "Marching with the bee-keepers to present a petition to Downing Street calling for more research investment in Colony Collapse Disorder was a particular highlight."

Last week during the reciprocal visit Dr Gibson visited Mark’s laboratory at the John Innes Centre.  As former Dean of Biological Sciences at UEA, he is keen to encourage science and improve the career structure for young scientists.

“The John Innes is internationally well known, producing internationally important science and scientists, and I particularly admire the dedication and enthusiasm of the young people in the lab, and their desire to advance their skills, knowledge and interest in their subject,” commented Dr. Gibson, who helped to start the scheme in 2001, and has taken part every year.

 “Without scientific research and a knowledge of how things work then policy decisions in science would be much poorer”

Mark’s research looks at the proteins produced by certain pathogens when they attempt to infect plants and humans.  The precise structure of these proteins can give an indication of how they cause disease, but because they are so small they cannot be seen, even with through conventional microscopes.  However, by purifying and then crystallising the proteins, it is possible to work out their structure using X-rays.  On the visit to Mark’s lab, Dr Gibson was able to help set up a crystallisation experiment.