National Crystallization Center
The National Crystallization Center was awarded an NIH NIGMS R24 grant to become a National Resource for crystallography in 2021. As the National Crystallization Center, we support academic, government, and non-profit research institutes, providing unique protein crystallization services for structural biology. Since it began operations in February 2000, the Crystallization Center has set up over 25 million crystallization experiments on more than 18,000 biological macromolecules for almost 2,000 laboratories worldwide. Macromolecular crystallization services at UB-HWI enable experiments that are monitored with state-of-the-art imaging techniques, empowering the detection of crystals that other techniques miss
Crystallization Screening at UB-HWI provides:
- Expert staff – Dr. Sarah EJ Bowman has been directing the Center since being recruited to UB-HWI in 2017 and works with a growing team of scientists that have been doing structural biology for close to two decades. Learn more about our team.
- State-of-the-art instrumentation – Brightfield (visual), second-order harmonic, and UV-two photon excited fluorescence techniques in a Rock Imager 1000 with SONICC are used, so no crystal is missed.
- Timely access – Runs are scheduled in advance on a monthly basis with multiple setup windows.
- A history of success – The Center has worked with academic, non-profit, government and industry users, and has screened over 18,000 proteins for over 2,000 laboratories worldwide.
News from the Crystallization Center
- As of Dec 11, 2025, there is a RAR compatibility issue for Windows 10/11. If you use Windows, please download the patched version of MARCO Polo that supports the newere RAR 5 archives.
- With the new website, the new submission form is live! Please use the link below to provide details about your sample. If you run into any difficulties, please reach out via email to us at getacrystal@buffalo.edu.
- Interested in optimizing your crystal hits at the National Crystallization Center? We are looking for commissioning users! Please reach out to us at getacrystal@buffalo.edu if you want to learn more.
- Generation 22 of the 1536 high-throughput screen started in September 2024. To download the most up-to-date Marco Polo to view and score your images, click here to get to the GitHub page with version 0.2.1!
- What’s the best way to send your sample for crystallization screening? Here’s a new paper we recently put together with colleagues from synchrotrons and cryoEM centers to provide guidance on this topic!
- The Summer 2024 Workshops are finished, and we’ve posted the virtual Applied Crystallization Workshop video on YouTube!
- New paper and video out in Journal of Visualized Experiments highlighting the experimental protocols in the Crystallization Center.
- New paper out in Acta D describing the Crystallization Center operations.
Information for Upcoming Crystallization Screening Deadlines and Dates
Updated 8/31/2026
The National Crystallization Center is happy to announce the upcoming dates for high-throughput crystallization runs. Please note that experiments are invoiced after sample set up. If you need assistance, please reach out to us at getacrystal@buffalo.edu.
Sept 2026 Soluble (taking reservations)
- Reservation Deadline: Fri Sept 11th
- Package Acceptance & Plate Setup:
- Tues Sept 15th – Thurs Sept 17th
- Mon Sept 21st – Thurs Sept 24th
Oct 2026 Soluble (taking reservations)
- Reservation Deadline: Fri Oct 2nd
- Package Acceptance & Plate Setup:
- Tues Oct 6th – Thurs Oct 8th
- Tues Oct 13th – Thurs Oct 15th
Note: Samples are not set up on Fridays.
Crystal Information
How It Works
Check the above schedule and reserve a spot in the queue for an upcoming crystallization screening run by emailing getacrystal@buffalo.edu. When you are ready to send your sample (to arrive during the package acceptance dates) please fill out the submission form and email tracking details for your shipment.
General sample preparation recommendations can be found in our recent publication:
1,536 non-redundant crystallization conditions are used to screen your sample using the microbatch-under-oil method, providing an efficient sampling of chemical parameter space. Each condition is imaged using state-of-the-art Formulatrix Rock Imagers over a period of six weeks. Imaging modalities include visual (brightfield) and Second-Order Non-linear Imaging of Chiral Crystals (SONICC), which includes Second Harmonic Generation (SHG) and UV-Two Photon Excited Fluorescence (UV-TPEF) imaging. SHG and UV-TPEF imaging can identify biological crystals not picked up visually or those obscured by precipitate. Brightfield, SHG, and UV-TPEF images are integrated with analysis software provided as part of the crystallization screening service.
Reminder to Acknowledge the Crystallization Center and Funding Agencies
We are grateful that NIH funding enables us to provide efficient high-throughput crystallization screening to academic, non-profit and government laboratories at a reduced rate. Please remember to cite the appropriate grant funding for your crystallization screening experiments.
- We request that the NIH R24 National Resource grant is acknowledged in any publications. We suggest the following language: Crystallization at the National Crystallization Center at UB-HWI was supported through NIH grant R24GM141256.
Additionally, it would be helpful if the experimental methods reference the Crystallization Center using the most recent updated reference for the soluble and membrane screens.
These citations help us to track publications and PDB depositions, an important metric of productivity that will help secure future funding for the Crystallization Center.
The Crystallization Center Produces Results
Crystals of the Month
10/5/26Excited to feature a recent publication by HTX Center users in the Izard Lab at Scripps as Crystals of the Month!
SARS-CoV-2 protein crystallization screening
10/30/20The Crystallization Center has been a resource for structural biology providing enhanced high-throughput crystallization screening for SARS-CoV-2 protein samples. Dr. Sarah Bowman gave a
lightning talk update on our progress at the COVID Commons with the Northesat Big Data Innovation Hub! We are providing crystallization screening experiments through our NSF RAPID funding.
Featuring our new crystal hunting software – MARCO Polo! Explore your crystallization parameter space with MARCO Polo! Open-source and on GitHub –
available to download.
MARCO Polo: Finding Crystals
9/30/20Summer intern Ethan Hollerman won a Student Poster Prize at the 2020 LCLS/SSRL Users’ Meeting for his work on implementing the MARCO algorithm into a new GUI! MARCO POLO is a multi-platform open-source Python-based graphical user interface that has been developed to provide access to MARCO automated classification and data management tools for biomolecular crystallization screening.
MARCO is an academic and industry collaboration using image data from the Crystallization Center, Bristol-Myers Squibb, GalaxoSmithKline, Merck, and the Collaborative Crystallization Centre in Australia. It involved image analysis experts at Google Brain, The University at Buffalo, Duke University, and the University of York in the UK, with industry input from Formulatrix. MARCO is being actively used in industrial settings, in Formulatrix instruments, and soon for users of the Crystallization Center. The GUI is undergoing beta testing, a paper is forthcoming, and the GUI will be released shortly.
Supporting SARS-CoV-2 Research
6/24/20The COVID-19 disease caused by the SARS-CoV-2 coronavirus has become a pandemic health crisis. An attractive target for antiviral inhibitors is the main protease 3CL Mpro due to its essential role in processing the polyproteins translated from viral RNA. The Crystallization Center worked with samples from Oak Ridge National Laboratory to help a study on room temperature X-ray structure of unliganded SARS-CoV-2 3CL Mpro. Inital crystal hits helped the researchers determine the ligand-free structure of the active site and the conformation of the catalytic site cavity at near-physiological temperature. They note comparison with previously reported low-temperature ligand-free and inhibitor-bound structures suggest that the room temperature structure may provide more relevant information at physiological temperatures for aiding in molecular docking studies.
Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography Kneller, DW,
et al Nat Commun 11, 3202 (2020).
More about the National Crystallization Center