The Structural Biology Center (SBC) is a national user facility for macromolecular crystallography at the Advanced Photon Source (APS).

SBC has closed operations to make way for a new resource called eBERlight -a virtual collaborative access team for the BER community. Capabilities from X-ray macromolecular crystallography to X-ray absorption spectroscopy will be available at the APS in Spring 2024.

SBC Highlights and News 

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

The APS uses advanced instrumentation, state-of-the-art software and methods and high throughput technologies. SBC, now eBERlight 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. Thanks to recent advances, faster detectors, and automation, one does not need not be a macromolecular crystallographer to take advantage of these facilities; our experienced staff are available to guide even novice users through the entire process.



Publications Highlights

Epitopes recognition of SARS-CoV-2 nucleocapsid RNA binding domain by human monoclonal antibodies. Kim Y, Maltseva N, Tesar C, Jedrzejczak R, Endres M, Ma H, Dugan HL, Stamper CT, Chang C, Li L, Changrob S, Zheng NY, Huang M, Ramanathan A, Wilson P, Michalska K, Joachimiak A.iScience. 2024 Jan 19;27(2):108976. doi: 10.1016/j.isci.2024.108976. eCollection 2024 Feb 16. PMID: 38327783 

Structure-based design of SARS-CoV-2 papain-like protease inhibitors. Jadhav P, Huang B, Osipiuk J, Zhang X, Tan H, Tesar C, Endres M, Jedrzejczak R, Tan B, Deng X, Joachimiak A, Cai J, Wang J.Eur J Med Chem. 2024 Jan 15;264:116011. doi: 10.1016/j.ejmech.2023.116011. Epub 2023 Dec 5. PMID: 38065031

Structure and enzymatic characterization of CelD endoglucanase from the anaerobic fungus Piromyces finnis. Dementiev A, Lillington SP, Jin S, Kim Y, Jedrzejczak R, Michalska K, Joachimiak A, O'Malley MA. Appl Microbiol Biotechnol. 2023 Oct;107(19):5999-6011. doi: 10.1007/s00253-023-12684-0. Epub 2023 Aug 7.PMID: 37548665 

Structural basis of impaired disaggregase function in the oxidation-sensitive SKD3 mutant causing 3-methylglutaconic aciduria. Lee S, Lee SB, Sung N, Xu WW, Chang C, Kim HE, Catic A, Tsai FTF. Nat Commun. 2023 Apr 11;14(1):2028. doi: 10.1038/s41467-023-37657-9.PMID: 37041140

Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin. Wydorski PM, Osipiuk J, Lanham BT, Tesar C, Endres M, Engle E, Jedrzejczak R, Mullapudi V, Michalska K, Fidelis K, Fushman D, Joachimiak A, Joachimiak LA.Nat Commun. 2023 Apr 25;14(1):2366. doi: 10.1038/s41467-023-38031-5.PMID: 37185902

Sel1-like proteins and peptides are the major Oxalobacter formigenes-derived factors stimulating oxalate transport by human intestinal epithelial cells. Arvans D, Chang C, Alshaikh A, Tesar C, Babnigg G, Wolfgeher D, Kron S, Antonopoulos D, Bashir M, Cham C, Musch M, Chang E, Joachimiak A, Hassan H.Am J Physiol Cell Physiol. 2023 Jul 1;325(1):C344-C361. doi: 10.1152/ajpcell.00466.2021. Epub 2023 May 1.PMID: 37125773

Potent and selective covalent inhibition of the papain-like protease from SARS-CoV-2. Sanders BC, Pokhrel S, Labbe AD, Mathews II, Cooper CJ, Davidson RB, Phillips G, Weiss KL, Zhang Q, O'Neill H, Kaur M, Schmidt JG, Reichard W, Surendranathan S, Parvathareddy J, Phillips L, Rainville C, Sterner DE, Kumaran D, Andi B, Babnigg G, Moriarty NW, Adams PD, Joachimiak A, Hurst BL, Kumar S, Butt TR, Jonsson CB, Ferrins L, Wakatsuki S, Galanie S, Head MS, Parks JM.Nat Commun. 2023 Mar 28;14(1):1733. doi: 10.1038/s41467-023-37254-w.PMID: 36977673




Current Beamline Statistics

APS-U Capabilities 

New opportunities are now available at eBERlight

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

The Advanced Protein Characterization Facility (APCF) is open for users.  This state-of-the-art laboratory has a HTP structural biology pipeline composed of bioinformatics, robotic gene cloning, protein expression, purification, characterization, crystallization, and structure determination.  

To gain access, register with the user office and submit an ESAF for Sector 84.