Cristina Cecchetti, ESR7

Cristina Cecchetti is ESR7, works at Imperial College London, United Kingdom. Her subject is “Structural and functional studies of plant and fungal secondary active transporters”

Cristina picture-final-finalPlease tell us about yourself:

I come from Nemi, a small town close to Rome in Italy. I grew up in a family with a scientific background: my father used to teach physics and chemistry in high school and my uncle is a chemist and teaches chemistry and maths. I got a Bachelor Degree in Chemistry at Sapienza University of Rome, thanks to a deep interest in chemistry developed during high school.  During my undergraduate studies, I was fascinated by Biochemistry and Structural Biology and that is what I decided to study during my Masters at Sapienza University of Rome.

Since I was very interested in studying and working abroad after graduating with my Master Degree, I decided to apply for an Erasmus project to do an internship in a pharmaceutical company in the UK for six months. That experience gave me the chance to see the differences between doing research in academia and in a company and to work mainly in cell biology on Alzheimer disease.

Apart from science, I love many forms of art and during my spare time I enjoy spending time in museums and I try to be involved in social activities. I also like very much travelling, exploring, meeting people and learning about new cultures.

Why are you interested in science?

I guess that growing up surrounded by “scientists” helped me appreciate science since my childhood. I remember playing with some molecular models of sugars and DNA built by my uncle and practicing with his analytical balance. Thanks to this, I have never seen science as boring stuff I had to study for school, but actually something I could play with. I have always been curious and as a child and teenager I was strongly encouraged to ask questions and try to give an answer. I am interested in science because it continuously challenges me, since every answer often arises a new question. I like what science symbolizes: collaboration between different scientific fields and exchange of ideas between people with different expertise. I like the chance that science gives to everyone to contribute to everybody’s knowledge. It is indeed like a puzzle, even though you may think that your piece is too small, but yet without it the whole picture may not make any sense. Sometimes it is not easy, but you have always the chance to try again and learn from your mistakes.

 Please tell us about your PhD project:

I am working on two membrane proteins (named UapA and AtBor1) that are responsible of carrying important nutrients from one side to the other of the membrane, for this reason they are named transporters. The main project focuses on the plant transporter AtBor1 that is required for transport of Boron (B) from root cells to the xylem for the distribution around the plant. Whereas UapA is a fungal transporter of uric acid and xanthine, important for the metabolism of nucleobases.

B is an essential micronutrient for plants and both deficiency and excess of borate in the soil are toxic to a range of important crop plants including wheat, barley and rice. In many regions throughout the world, the yield and the quality of crops are challenged by this problem.

Figure Cristina - example of protein crystals
Example of protein crystals

Since we want to understand the transport mechanism of AtBor1 and UapA, the most informative way to study it is by looking into their 3D structure, combined with techniques useful to investigate their function.  We start by “producing” (expressing) the proteins and purifying them in order to have a sample with a very high quality and purity. Then the goal is to use a technique called X-Ray crystallography that allows to determine the 3D structure of a protein by detecting the signal due to the interactions between the protein and X-Rays. In order to get a good signal, we need to find the conditions necessary to have the protein in form of good-sized and regularly-shaped crystals, process that usually needs many trials and a good optimization.

 

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

I like that we are part of a big network spread around Europe. Even though we all have our specific PhD projects to focus on, we have the same communal aim to Rationalize Membrane Protein Crystallisation (RAMP). We all come from different scientific backgrounds and being part of a network gives the chance of relying on each other’s expertise and exchanging ideas. Furthermore as part of our PhD we have to spend some time working in other laboratories within the network that allows to learn new techniques, to improve the ones already in use and to meet new people within the scientific community.