The Structural Biology Center (SBC) is a national user facility for macromolecular crystallography at the Advanced Photon Source. The facility uses advanced instrumentation, state-of-the-art software, and methods and high throughput technologies.

SBC continues to research for therapeutics and treatments to combat COVID-19. Scientists at SBC and APS received an ANL impact award on its 2020 research encompassing the SARS CoV-2 virus.

SBC Highlights and News 

The facility uses advanced instrumentation, state-of-the-art software and methods and high throughput technologies. SBC is capable of addressing the most challenging projects in structural biology that include: large macromolecular assemblies (ribosomes, viruses, regulatory protein/DNAcomplexes), membrane-bound and membrane-associated proteins (ion channels, receptors, integrins). Structures of enzymes and complexes with ligands and inhibitors can be determined at atomic resolution.

The Structural Biology Center enables the atomic-scale study of macromolecular systems using very small crystal samples. It also offers the most efficient data collection and structure determination systems for protein crystallography worldwide. Thanks to recent advances with larger, faster X-ray detectors and automation of laboratory processes for expressing proteins and growing crystals, the time required to solve molecular structures has been greatly reduced. Research that not long ago took months or years may now take only hours. In addition, one need not be a macromolecular crystallographer to take advantage of these facilities; our experienced beamline staff are available to guide even novice users through the entire process.



Publications Highlights

Data collection from crystals grown in microfluidic droplets. Babnigg G, Sherrell D, Kim Y, Johnson JL, Nocek B, Tan K, Axford D, Li H, Bigelow L, Welk L, Endres M, Owen RL, Joachimiak A.Acta Crystallogr D Struct Biol. 2022 Aug 1;78(Pt 8):997-1009. doi: 10.1107/S2059798322004661. Epub 2022 Jul 21.PMID: 35916224

Potent and Selective Covalent Inhibition of the Papain-like Protease from SARS-CoV-2.Sanders B, Pokhrel S, Labbe A, Mathews I, Cooper C, Davidson R, Phillips G, Weiss K, Zhang Q, O'Neill H, Kaur M, Ferrins L, Schmidt J, Reichard W, Surendranathan S, Parvathareddy J, Phillips L, Rainville C, Sterner D, Kumaran D, Andi B, Babnigg G, Moriarty N, Adams P, Joachimiak A, Hurst B, Kumar S, Butt T, Jonsson C, Wakatsuki S, Galanie S, Head M, Parks J.Res Sq. 2022 Jul doi: 10.21203/ Preprint.PMID: 35898342

The first crystal structure of a xylobiose-bound xylobiohydrolase with high functional specificity from the bacterial glycoside hydrolase 30 subfamily 10. St John FJ, Crooks C, Kim Y, Tan K, Joachimiak A.FEBS Lett. 2022 Jul 25. doi: 10.1002/1873-3468.14454. Online ahead of print.PMID: 35876256

A Genomic Island of Vibrio cholerae Encodes a Three-Component Cytotoxin with Monomer and Protomer Forms Structurally Similar to Alpha-Pore-Forming Toxins.  Herrera A, Kim Y, Chen J, Jedrzejczak R, Shukla S, Maltseva N, Joachimiak G, Welk L, Wiersum G, Jaroszewski L, Godzik A, Joachimiak A, Satchell KJF.J Bacteriol. 2022 May 17;204(5):e0055521. doi: 10.1128/jb.00555-21. Epub 2022 Apr 18.PMID: 35435721

Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin. Osipiuk J, Wydorski PM, Lanham BT, Tesar C, Endres M, Engle E, Jedrzejczak R, Mullapudi V, Michalska K, Fidelis K, Fushman D, Joachimiak A, Joachimiak LA.bioRxiv. 2022 Apr 25:2021.09.15.460543. doi: 10.1101/2021.09.15.460543. Preprint.PMID: 35547846

Functional and Structural Characterization of Diverse NfsB Chloramphenicol Reductase Enzymes from Human Pathogens.   Mullowney MW, Maltseva NI, Endres M, Kim Y, Joachimiak A, Crofts TS.Microbiol Spectr. 2022 Feb 23:e0013922. doi: 10.1128/spectrum.00139-22. Online ahead of print. PMID: 35195438

Expanding Benzoxazole-Based Inosine 5'-Monophosphate Dehydrogenase (IMPDH) Inhibitor Structure-Activity As Potential Antituberculosis Agents. Chacko S, Boshoff HIM, Singh V, Ferraris DM, Gollapalli DR, Zhang M, Lawson AP, Pepi MJ, Joachimiak A, Rizzi M, Mizrahi V, Cuny GD, Hedstrom L.J Med Chem. 2021 Dec 23;64(24):18233-18234. doi: 10.1021/acs.jmedchem.1c01923. Epub 2021 Dec 2.PMID: 34855408



Current Beamline Statistics

APS-U Capabilities with SBC and eBERlight

SBC is seeking collaborators interested in exploring other tools at the APS, such as macromolecular structural dynamics and imaging of soils, plants, or aerosol particulates. If you are interested, please contact

New opportunities are now available at SBC with Serial crystallography (SSX).

The APS-U will provide a highly brilliant beam ideally suited for serial crystallography methods.  Serial crystallography methods have many advantages: they are more biologically relevant at room temperatures and reduce radiation damage by order of magnitude per structure. It also encourages the use of small or x-ray sensitive samples with the ability to perform time-resolved measurements.  Advances in SSX experiments are paramount for the APS-U. This method is expected to flourish with the significant increase in x-ray flux density and a concomitant rise in multi-crystal datasets.  If you are interested, please contact Karolina Michalska (   Recent publication: 2'-O methylation of RNA cap in SARS-CoV-2 captured by serial crystallography.

The 2022 APS/CNM 2022 Users Meeting will held on May 2-6, 2022 and May 9-13, 2022. 

APS/CNM 2022 Users Meeting

See the 2021 APS/CNM Users Meeting archives below.

2021 Users Meeting Program Information | Advanced Photon Source (

May 6, 2021 
APS Training #6:  Dynamic X-ray Crystallography, Darren Sherrell (co-organizer)

May 11 & 12, 2021
APS WK#9:  Advances in COVID-19 Prevention and Treatment Enabled by Structural Biology Research, Karolina Michalska (co-organizer)

APS Overview Virtual Tour