Photo:

Sam Horrell

Its been a pleasure. Feel free to keep asking questions.

Favourite Thing: There are lots of things I love about science but the main thing is the challenge of solving a puzzle. Why is this not working? How can I make this work better? Why did this work last time and not this time? The most interesting science is when it’s all going wrong.

My CV

Education:

Qualifications:

Upper second class Bsc (hons) in medical biochemistry from The University of Leicester

Work History:

A Pet Shop. Cleaning my school in the evening and summer. Summer studentship at the University of Leicester.

Current Job:

PhD Student

Employer:

The Univeristy of Liverpool/ Diamond light Soruce

Me and my work

I produce protein samples for structural analysis, focusing on the use of long wavelength X-rays to generate 3D models of proteins.

As a structural biologist my work involves the use of biology, chemistry and physics to achieve my goals. To produce a 3D structure of a protein we fire X-rays at crystals and these produce a pattern that can be recorded. These patterns contain information about how a protein looks but they don’t have everything we need. A synchrotron is effectively a giant microscope for X-rays, but without all the information it is impossible to focus it and see your protein. My project involves the use of a special type of X-ray and experimental set-up to retrieve this lost information and bring the structures into focus.Using these special types of X-rays brings about a whole mess of complications that I’m helping to overcome.

As well as helping in the development of this technique I am also working on solving the structure of a protein involved in the development of cancer in humans. For many years crystallography has been a key technique in figuring out exactly what a protein does in the body, what they interact with and how genetic mutations or infections cause disease. It’s particularly useful in finding out how drugs work on proteins. I hope that by finding the structure of this protein I will be able to see how exactly this protein acts in the body to cause cancer and see how we can prevent this.

My Typical Day

Growing bacteria and breaking them open to get protiens to fire X-rays at. Making lots of colourless solutions.

The great thing about working in structural biology is a typical day is difficult to define because there are so many aspects to consider.

Some days it will be straight to the microbiology lab where I would be genetically modifying bacteria to produce a specific protein I’m interested in. Once I’ve done that I can burst open the bacteria using sonic waves or high pressure, this release all the proteins in the cell and it’s now my job to isolate that one protein I want. This may sound quick but it can take weeks, months or years  to get your protein alone. If you work hard enough or are lucky enough you’ll get your protein alone and be able to produce a crystal from it.

Once you’ve got a crystal a typical day is very different, this is when you get to head over to the synchrotron and fire X-rays at your protein and hopefully produce a 3D model of  your protein. No genetic modification but you do get to use a robot, radiation and a building over 0.5K in circumference kicking out 3GeV of energy. The days after this involve a lot of computer work to analyse the pattern and get your missing information to focus the artificial microscope and see your protein. Hopefully this tells you something about how the protein works, because structure is function.

What I'd do with the money

Buy a netbook and camera so I can blog on the go and get some pretty pictures along the way.

When I started my PhD I thought it would be good to keep a blog of my experiences during my 4 years study. In the beginning this went well, the aim was about one post a month on some aspect of crystallography but as I’ve gotten busier it has been more and more difficult. Particularly as my laptop is rather large and frequently refuses to charge so I cannot use it on the go. A small netbook would be very useful in this respect. All the current photos on my blog have been from my phone, although the quality is not bad it leaves a lot to be desired.

Please check out my blog at http://justanotherphdstudent.blogspot.co.uk/

It is aimed at an A level/ undergraduate audience so don’t worry if you find it difficult to read at times.I’m more than happy to answer any questions you may have. That’s what I’m here for after all.

 

My Interview

How would you describe yourself in 3 words?

Geek, excitable, human.

Who is your favourite singer or band?

Biffy Clyro.

What's your favourite food?

Mexican.

What is the most fun thing you've done?

Surfing in California, playing a gig in Leicester Square or playing ultimate frisbee.

What did you want to be after you left school?

A Doctor.

Were you ever in trouble in at school?

Once or twice.

What was your favourite subject at school?

Biology.

What's the best thing you've done as a scientist?

Not my best thing but my best story is probably when I accidently set a pipette on fire.

What or who inspired you to become a scientist?

Partly because I enjoyed the subject the other part is probably down to watching too much science fiction and thinking damn that looks cool.

If you weren't a scientist, what would you be?

Probably a science teacher.

If you had 3 wishes for yourself what would they be? - be honest!

To complete my PhD. To get super powers from a freak science accident. To live a long happy life.

Tell us a joke.

Just imagine a T-rex trying to make a bed.

Other stuff

Work photos:

This is a picture from inside the synchrotron, the different coloured blocks are all different types of magnets that push, pull and squeeze electrons to make them fire out X-rays myimage2

Once X-rays have been generated by the magnets they enter the experimental hutch, pictured below. The protein crystal is on the little pin in the centre.  myimage3

Here’s a closer look at what these protein sample might look like.

myimage4 myimage5 myimage6

From these crystals we get diffraction patterns that look something like this

myimage7

and from those spots we can get structures like this one of haemoglobin

myimage8