Piotr Wilk, PhD, moved from Berlin to Krakow to join our team. Previosly Piotr worked as a Research Scientist at Macromolecular Crystallography Group in Helmholtz-Zentrum Berlin. We are happy to have another such experienced specialist in our team. Read what Piotr says about himself.
I have developed my fascination with biochemistry during my studies at the Rzeszów University of Technology where I got my training in chemical technology. The subject of my MSc was synthesis of new compounds with potential biological activities. In 2008 I have abandoned organic chemistry and moved to Warsaw, where in the Laboratory of Comparative Enzymology at the Nencki Institute of Experimental Biology I have investigated various avenues of biochemistry. One of them was structural analysis of an enzyme. Getting my first protein crystals, solving its structure and analyzing the results was an unforgettable experience. After all not every day one has an opportunity to have a glimpse at something no one else has seen before and to broaden our understanding of the surrounding world. After completing my PhD in late 2013 I decided to follow my professional hobby which was crystallography. The best places to play with crystals are synchrotron sites where the vast majority of the diffraction data resulting in PDB depositions are collected. Since 2014 I was employed by the Humboldt University in Berlin as a Post-Doc in frames of Berlin Joint MX-Laboratory working in MX group at the BESSY II electron storage ring. Joining the group of experts fulfilled my expectations to over 100%. From my colleagues, I learned a lot about preparing, handling, measuring and analyzing crystals and protein structures, but also about operating synchrotron beamlines and sustaining their very complex functionalities.
The character of my work allowed me to gain a deep insight into all aspects of crystallography from the perspective of facility user running my own research project, through various collaborations and also as user support. Meeting scientists from all corners of (nota bene roundish) world I could observe and learn different approaches to solving difficult problems. I have also learned about alternative routes of investigating three-dimensional structures of macromolecules such as Cryo-EM. After five years in Berlin, I took an opportunity to join an enthusiastic group at the Malopolska Centre of Biotechnology in Kraków. Since April 2019 I am a postdoctoral researcher at the Structural Biology Core Facility, a group employing multilateral approach to structural biology.
In my humble opinion, structural biology is the most fascinating of all stirring scientific disciplines. It is also one of the fastest developing ones with a number of entries to the Protein Data Bank growing exponentially. Crystal structures allowed us to gain insight in the mysteries of protein functionalities. We could understand how tiny conformational changes in hemoglobin allow it to bind oxygen cooperatively, transport and release it just where it is needed. We elucidated how the world’s smallest rotary engine of ATPase works to provide our cells with crucial energy carrier. We could understand how the energy of our favorite star is captured in photosystem II to fuel essentially all life forms on earth. We learned about mechanisms of countless enzymes and receptors starting with lysozyme. Most importantly we use this knowledge not only to expand our understanding of the creation but also to support the design of novel medicines effective against diseases deadly just a few years ago and now relatively easily treatable such as HIV infections or number of carcinomas. I am happy if I can add a tiny brick to this marvelous pyramid of science.
In private I am a proud father of two wonderful young ladies and in my free time, I enjoy small pleasures such as good book, movie or journey.
