X-ray Precision: Thanks and Farewell, Dr David Briggs

We bid a fond farewell to charismatic crystallographer Dr David Briggs, tweeting live from the University of Manchester in this International Year of Crystallography.  Coincidentally, this was also the week of a famous and pioneering crystallographer,  Nobel Laureate Dr Dorothy Hogkin’s birthday. Dorothy Hodgkin was responsible for decoding many early protein structures, including insulin.

 

What is crystallography? Well, we’ll let Dr Dave explain in his own words:

“Shooting X-rays at crystals’ sounds like the most fun ever and something out of a science fiction battle, in fact, many countries now build synchrotrons to help them produce the X-rays needed for such work. Crystallography is a hugely important process in determining structures of proteins, which in turns allows us to identify where we can target drugs to treat diseases. David’s own work on arthritis looks at possible drug targets to help treat this curiously modern disease.  Most of these structures are also freely available, as David pointed out, in the Protein Data Bank, which also reached 100,000 structures this week.100000PDB

Dave’s lab is  a typical molecular biology lab space; small, crowded with solutions and very precisely regulated!  If you know a molecular biologist, or protein chemist, this is what their work place looks like. Those funny blue things are Gilson pipettes that help deliver tiny microlitre quantities of solutions for the very tiny experiments of structural biology.

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As well as taking us on a tour of how to make tiny protein crystals, David found himself in JRR Tolkien’s old haunts in Kirkwood.  We thanks David for his awesome week of molecular biology, be sure to follow him on his adventures on his regular account, @xtaldave, or via his about.me profile. If you missed out on anything, catch up via RealScientists on Storify.

Next week: @UWBiostat Outreach Manager and @CienciaPR vice-director, Dr Mónica Feliú-Mójer aka @moefeliu.

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Dr David Briggs brings some Structure to Real Scientists!

Dave-QEDThis week we are pleased to welcome Dr David Briggs to the @realscientists steering wheel.  David is a Post Doctoral Researcher at the University of Manchester, UK, and answered our welcome-exam questions with style.

Why/How did you end up in science?

Science is the only thing I’ve ever been any good at, academically speaking. My Dad is a vet, and with his influence I think I was always going to so something in the life sciences field. My interest in chemistry at A-level (16-18) lead me to study biochemisty at University in Birmingham.

Why did you choose your current field and what keeps you there?

Whilst at Birmingham, I became fascinated by protein structure and function. My final year project was a protein structure modelling project, and my supervisor suggested that I go for a Masters degree in Structural Biology at Birkbeck College in London. Whilst there I was given the opportunity to go for a PhD, which I took. The rest, as they say, is history. The real appeal of solving protein structures is that until you tell someone or publish the structure, you’ve been the first human being ever to see what that protein looks like, and to see how it folds, and how its structure relates to its function. I imagine it’s the closest I’m going to get to finding out that I’m pregnant. Until I tell someone, that’s my little secret. That’s kind of cool .

Tell us about your work?

I’m a structural biologist/biophysicist, studying molecular mechanisms of arthritis at the University of Manchester, UK. I primarily use protein crystallography to study what the protein molecules inside us look like, and how their structures are related to their various functions. In addition to this, I uses various biophysical techniques to examine how proteins interact with each other to regulate their different functions. Currently, I’m studying a complex proteoglycan (a molecule composed of proteins and sugars) found in our blood stream. This molecule (called Inter-alpha-inhibitor, or “IaI” for short) can leak into our joints during as a result of inflammation caused by diseases like osteoarthritis. I’m currently trying to figure out whether or not the IaI in arthritic joints is a good thing – it is part of the bodies attempt to repair damaged cartilage tissues or is it part of the problem – does it damage the cartilage? This work is funded by Arthritis Research UK.

Motivation: why should the lay public care about your research?

IF you live long enough, YOU ARE GOING TO GET ARTHRITIS. The load bearing structures in our joints like cartilage haven’t evolved to support us for our 80+ year life spans. It’s also likely that you aren’t going to get arthritis before you have had children, so there is no selective pressure to evolve joints that can regenerate. By the time the disease has hit, you’ve already passed on your genetic information to the next generation. The World Health organisation estimates that 9.6% of men and 18.0% of women aged over 60 years have symptomatic osteoarthritis. As populations age and working age extends into later life, this is going to have a significant burden on our healthcare systems. At the moment, Arthritis can only be treated symptomatically. Anything we can do to understand the progression of Osteoarthritis is going to help future drug design efforts.

Any interesting hobbies you’d like to share?

When not doing science, I look after my two sons: James (10) and Harry (7). I also have a very sporadic blog, a crippling addiction to coffee and an out-of-control twitter habit. I enjoy real ale, cooking, and eating what I’ve cooked. Washed down with real ale, of course. I then walk up hills in a vain attempt to shed the pounds.

How would you describe your ideal day off?

Late start. Cooked breakfast. Long country walk to a decent pub for lunch. Boozy pub lunch. Walk home again. Fall asleep by the fire with a glass of a good peaty malt whisky. Heaven.

Now that is an admirable day off.  Please welcome Dr David Briggs/@xtaldave to Real Scientists!