Diogo Melo, ESR 8

Diogo works at the Center foto cortadafor Free Electron Laser Science (CFEL) in Hamburg, Germany.

His subject is Controlled growth of uniformly sized microcrystals, optimised for time-resolved crystallographic experiment.

On Twitter: @Monrroy_Melo

Tell us about yourself

I come from Alguber, a small village in Portugal that mostly lives off agriculture, in which I used to work most of the summers. I studied biochemistry for four years in the University of Algarve and two years in NOVA University of Lisbon… the last year I worked with X-Ray crystallography. Between those two periods, I worked for almost a year as a door to door telecommunications salesman (yes, one of those!) to save money for the Masters degree.

I feel passionate about biochemistry, structural biology and X-Ray crystallography. I also enjoy showing others how fascinating science can be, mostly in person talks in events like “The European Researchers’ Night”. I also love strategy games (like chess) and electronic music.

Why are you interested in science?

I’ve always been interested in knowing how things work, and science for me is a never-ending puzzle – following the answers, are always new questions. When science puzzles are solved, significant improvements for society can be made. The possibility of even the tiniest contribution to society greatly fulfills me, therefore I take great joy in this work.

Tell us about your PhD project

My work involves X-Ray crystallography, which is a technique used to solve protein 3-D structures.

Proteins are responsible for most functions inside every living being known until now. To understand how proteins perform their function, knowing their 3-D structure is fundamental. Unfortunately, because proteins are so small, knowing the protein’s structure is not easy, and it cannot be done through direct means – for example, normal microscopes.

The most successful technique to discover a proteins’ structure is X-Ray Crystallography. This technique is based upon purifying enormous protein quantities and then obtaining a pure protein crystal. These crystals are then measured with X-Rays and we obtain a 3-D “snapshot” of the protein. From the 3-D “snapshots”, scientists can think about how the protein executes its function, but sometimes, it is so complex that “snapshots” are not enough.

To address this problem, time-resolved X-Ray crystallography can be used. This technique obtains many protein 3-D “snapshots”, often on very short Flying-subtitletime-scales, for instance, over femtoseconds (which is 0.000 000 000 000 001 seconds!). After we obtain the many 3-D “snapshots”, we put them together following a time-line, in the end obtaining a “movie”. Imagine taking a picture of a bird flying every half a second and then putting them together, this results in a movie where you can watch how the bird’s wings bend. This is the case for proteins, we can now obtain “movies” of proteins performing their function and better understand how they work.

What do you or did you enjoy most until now in your position within RAMP network? Why ?

By far I enjoyed mostly the potential of knowledge interchange between the various collaborators. The RAMP network comprises researchers and institutions from across not only Europe, but also North America, Asia and Australia. People from different cultures and experiences, are working together to solve a scientific problem by different approaches. I think that such an environment has great potential, I hope it continues to grow and strengthen itself and feel privileged to be part of it.

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