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I am interested in a protein found in our blood called “Inter-alpha-Inhibitor” (I-alpha-I for short).  When we get Arthritis (or other joint injuries and diseases) this protein gets into our joints. At the moment, we don’t know if this is a good thing or a bad thing.

It might be trying to repair our joints, or it might be making them worse!

We are looking at the 3D structure of this protein, and how this protein affects cells in the joint to try and figure out what it is doing, whether it is “friend or foe”.

If it turns out it is a friend – then that’s great – we could perhaps inject more of it into the joint to speed up the repair process.

If it turns out to be a foe, we can try and find ways of stopping it getting into the joint, or stopping it doing harm once it is there.

In the end, we want to try and help people with arthritis get better, faster.

I’m a crystallographer and a biophysicist, so I tend to spend a lot more time in front of a computer than most biologists. I also drink an obscene amount of coffee to try and keep me going through the day!

I spend quite a lot of time making my own reagents to conduct experiments – these are normally proteins or bits of proteins that we are interested in studying.

Having made the proteins, I can then go and test their activity on all sorts of equipment – I am mostly interested in which other proteins my proteins stick(bind) to – when proteins bind to one another there is often a functional result that might be important for the disease I am studying – so it is really important that I understand this for my protein.

I am also a crystallographer, which means that I use crystallography to understand the precise structure of my protein, down to where the individual atoms within the protein sit. In order to do this, I crystallise my proteins(s) using amazing crystallisation robots – these machines can fire a 50 nanolitre drop (50 billionths of a litre) of protein solution accurately onto a spot the size of a pinhead. We can setup thousands of crystallisation experiments every hours – and the more experiments we setup, the more likely we are to be able to grow crystals of our protein!

When we get crystals, we take them to Synchrotrons (mini versions of the large hardon collider – the one near Oxford is “only” 560 metres around, rather than 27 kilometres for the LHC), and shoot these crystals with high powered X-ray beams. This gives us diffraction data which then allows us to figure out what the protein looks like!

Sounds simple. Can take years!