Elham Vahdatahar is ESR1, she works at Grenoble University in France. Her subject is “Optimisation of crystal growth using a microfluidic technology-based crystallisation bench”.
Please tell us about yourself:
I was born in Ahwaz, Iran. I studied cellular and molecular biology (genetics) at Isfahan University and then I chose to study biophysics at the University of Tehran. My master thesis was about the effect of potassium sorbate and vitamin C on fibrillation of bovine serum albumin.
I really like to know more about proteins; they are molecules ensuring the fulfillment of the majority of cellular functions such as molecular recognition (immune system), signaling pathways (hormones), metabolite and nutrient transport, as well as catalysis of biochemical reactions (enzymes). The function of proteins derives from their three-dimensional structure, i.e., how the amino acids of the polypeptide chain are arranged in relation to one another in space. It is only in its folded state (native state) that a protein can exert its biological activity. Knowledge of the structure of proteins is therefore essential to understanding their functioning mechanism and facilitates our perception of their involvement in certain fundamental biological processes. I wonder how different conditions can affect protein structures and functions and finally how we can get more information on that.
Also, I like to play ping pong. I am an amateur pianist and I wish to progress beyond amateurism by practicing it.
Why are you interested in science?
When I was a child there was a television series called “The Magic School Bus”. In every episode students with their teacher (Ms. Frizzle) were going on field trips and learning so many things about different aspects of science. My mother was an experimental science teacher and as a child, she was like Ms. Frizzle for me. We didn’t have the magic bus but we had magic pocketbooks and we had so many field trips. I think this is the main reason why I like science. When I grew up and went to school and then university I realized that experimental science is something that really makes me happy. I believe science is like a puzzle and I love to piece together complicated puzzles to find the answers and questions behind them.
Please tell us about your PhD project:
If we consider the body as a complex machine, proteins are part of this machine that should work properly so the system doesn’t encounter a problem (disease). As mentioned earlier, to understand how a protein works, we need to know its three-dimensional structure. Protein crystallography is one of the most relevant methods to study this structure. This method requires crystals with appropriate size and good diffraction quality. A crystallization bench was designed in our lab a few years ago for this purpose. By means of this device we can control various physico-chemical parameters (e.g. temperature, chemical composition) during the crystallization in order to optimize the crystallization condition to get bigger crystals or uniform population of tiny crystals. The main challenge of my PhD project is to pursue development of the crystallization bench and to adapt it for crystallization of membrane proteins.
Another objective is the integration of the in situ UV spectroscopy to investigate multidimensional phase diagrams and use of the statistical modeling to rationally improve the latter stages of membrane protein crystallization. As a consequence we will be able to grow appropriate crystal samples of membrane protein and know more about their structures by using the Neutron Macromolecular Crystallography and fast (sub ms) time-resolved X-ray crystallography.
What do you or did you enjoy most until now in your position within RAMP network? Why ?
I really like the goal of this network which is to find solutions to establish rational approaches in the crystallization of membrane proteins, and how professors, doctoral students and companies federate for the same objectives and work together to achieve this.