Structural Biology Core Facility

03/02/2026

It’s been quiet here for a while, but we are back with some fantastic news. The first crystallographic fragment screening campaign conducted by the SBCF team has just been published in Communications Chemistry!

https://www.nature.com/articles/s42004-026-01897-9

We purified protein and performed the optimization of crystallization conditions at SBCF, then traveled to the MAX IV Laboratory in Lund to carry out crystal soaking and measurements using their state-of-the-art infrastructure. Finally, the comprehensive data analysis was completed back at our facility.

If you are interested in performing a crystallographic fragment screening campaign on your protein, please contact us directly!

Illustration: Dominika Dobosz Małopolskie Centrum Biotechnologii

12/11/2025

We are pleased to announce the appointment of Dr. Piotr Wilk as the new Head of the Structural Biology Core Facility (SBCF) at MCB!

Dr. Wilk succeeds dr hab. Przemyslaw Grudnik in this leadership role, bringing extensive expertise in macromolecular crystallography and user operations.

Dr. Wilk earned his Ph.D. from the Nencki Institute of Experimental Biology PAS in 2013. He gained crucial technical experience working in the Macromolecular Crystallography at HZB at the Helmholtz-Zentrum Berlin (HZB) synchrotron and Humboldt-Universität zu Berlin.

He joined Jagiellonian University and MCB in 2019 as a Postdoctoral Researcher within the TeamTech Core Facility FNP project and has since been an integral part of the SBCF team. His high productivity is evident in his contributions to nearly 60 structures deposited in the RCSB Protein Data Bank since joining MCB.

Dr. Wilk is a specialist in protein crystallography and crystallographic fragment screening. He is responsible for coordinating all our synchrotron measurements and has led structural analyses in numerous collaborative projects, including specialized 'gene-to-structure' projects and commercial collaborations. His commitment to research is further demonstrated by his current leadership of an OPUS grant funded by the NCN National Science Centre. This project is focused on structure-based targeting of antibiotic resistance in bacteria by inhibiting the post-translational activation of the translation factor EF-P – a crucial process in dangerous Gram-negative pathogens.

Under Dr. Wilk’s leadership, the Structural Biology Core Facility will continue to provide state-of-the-art infrastructure and essential expert support for structural research at MCB.

Join us in congratulating Dr. Wilk on his new appointment! We look forward to the continued advancement of structural biology research and the amazing structures solved at MCB under his expert direction. 👏

Uniwersytet Jagielloński

24/07/2022

Exciting (and really hot☀️) day ahead of our team. Today we are measuring for our users at the European Synchrotron Radiation Facility - ESRF ID-23 beamline🇫🇷.

Hoping for some nice diffraction and that neither crystals nor our team will melt today!

22/02/2022

The latest publications from our users 📣🎊 We look forward to the next articles.

1) Cryo-EM reconstructions of BMV-derived virus-like particles reveal assembly defects in the icosahedral lattice structure - https://pubs.rsc.org/en/content/articlelanding/2022/NR/D1NR05650F

2) Crystal structures of apo- and FAD-bound human peroxisomal acyl-CoA oxidase provide mechanistic basis explaining clinical observations - https://www.sciencedirect.com/science/article/pii/S0141813022002434?via%3Dihub

17/02/2022

An excellent opportunity for structural biologists to join a meeting highlighting recent discoveries in the field. Best speakers and cutting-edge knowledge guaranteed 👩‍🏫👨‍🏫 Attendance is free, but registration is required.
And one of the speakers is Sebastian Glatt :)

More information about the event - https://inext.iimcb.gov.pl/
Registration is open 🏃‍♀️

Are you interested in structural biology? 🧬🧪🔬 If yes, you should join the iNEXT-Discovery 2nd Annual Scientific Meeting.

🔗 More information: bit.ly/34JY2Pw
📝 Registration is now open: bit.ly/3GDVXSf

Helmholtz-Zentrum Berlin

11/02/2022

Today we are celebrating International Women in Science day. Below are some iconic women who impacted the field of structural biology, especially crystallography 💪👩‍🔬
❔ How many of them do you recognize? ❔
It's worth remembering that of seven women, who have won the Nobel Prize in Chemistry, two were crystallographers (Dorothy Hodgkin and Ada Yonath) 💎💎



---
Rosalind Franklin
Published numerous articles on the structure of tabacco mosaic virus. But she is most famous for refining the X-ray crystallography so precisely that she was able to capture the sharp image of DNA.

Kathleen Lonsdale
She confirmed the structure of the benzene ring, carried out studies of diamond, was one of the first two women to be elected to the Royal Society (in 1945), and was appointed the first female tenured professor at University College London

Dorothy Hodgkin
Pioneer in the work of the first X-ray photographs of crystalline proteins. She won her Nobel Prize in Chemistry in 1964 for the structures of penicillin and vitamin B12.

Isabella Karle
She was an expert in deducing the structure of molecules by observing the patterns in the deflected rays and developed the symbolic addition procedure that connects the theoretical "direct method" apparatus and actual X-ray diffraction data. Her work gave the basis for pharmaceutical researchers to understand the chemistry going on inside the body.

Olga Kennard
from 1965 until 1997 she ran the Cambridge Crystallographic Data Centre, an internationally recognized source of structural data on small molecules

Eleanor Dodson
was the main investigator behind CCP4, the collaborative computing project that currently shares more than 250 software tools with protein crystallographers worldwide

Based on:
https://www.nature.com/articles/505609a
https://www.nytimes.com/2017/10/26/obituaries/isabella-l-karle-dead-findings-on-molecules-helped-husband-win-nobel.html
https://royalsociety.org/topics-policy/diversity-in-science/scientists-with-disabilities/dorothy-hodgkin/

07/02/2022

Another publication of our users! Congrats Bionanoscience and Biochemistry Laboratory - Heddle lab

Cryo Electron Microscopy Structures of the new VLPs

Virus-like particles are promising for drug delivery systems and vaccine development, but controlling their size and morphology is challenging. Here, amino acid sequences are inserted into MS2 bacteriophage virus-like particles, with their size and shape being controlled by varying the insert used.

31/01/2022

The new special issue of Trends in Biochemical Sciences is fully dedicated to pushing the boundaries of Cryo-EM. 9 articles are focusing on recent advances but also touch the topics such as broader access to Cryo-EM through centralized facilities and using Cryo-EM in the drug discovery pipeline.
Link to the special issue - https://hubs.li/Q012PKg40



Cell Press

24/01/2022

2021 in numbers:

• 1283 plates set for crystallization
• 30 individual users for crystallography
• 15 synchrotron trips/ remote sessions
• 1793 crystals measured for our users
• Over 20 individual users prepared the grids for cryo-EM microscopes with SBCF
• 592 TB of data collected on Titan Krios (with Synchrotron SOLARIS)
• 1 624 367 images and tomograms collected on Titan Krios

and
• 91 – the number of crystal structures deposited so far by our users 🥳

Thank you for being with us in 2021! 🙌

#

20/01/2022

The calming and soothing sound of the working Phenix robot 🤖 for this cloudy day ☁️ The robot starts with loading the screen 🦾 Then it loads a protein solution to the wells in the plate, and at the end, it transfers buffers from the screen to the protein droplet 💎

14/01/2022

It comes as no surprise as protein structure prediction is the Nature Method of the year 2021. AlphaFold2 and RoseTTAfold are revolutionizing the work of structural biologists around the world 💻

A long-awaited method to predict 3-dimensional protein structure simply from the linear amino acids chain has finally arrived. Over the next years, we will learn in which direction structural biology develops. As multi-protein complexes, predicting protein dynamics, ligand binding, and function prediction are still a challenge we wait to see answers to that soon 🧐

The future is bright and another structural biology method chosen as a method of the year confirms that knowing the structure of your target protein is a key to answering many questions!

Method of the Year 2021: Protein structure prediction -
https://www.nature.com/collections/dfejabhghd


Nature

Method of the Year 2021: Protein structure prediction

12/01/2022

Once again we are proud of our users who publish their results in top journals! Congrats to Bionanoscience and Biochemistry Laboratory - Heddle lab from Małopolskie Centrum Biotechnologii

Link to the publication - https://www.science.org/doi/10.1126/sciadv.abj9424



Science Advances
Uniwersytet Jagielloński

An artificial protein cage can be programmed to disassemble on demand.