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

Transient complexes of the Nsp7, Nsp8 and Nsp12 in SARS-CoV-2 replication transcription complex. Wilamowski M, Hammel M, Leite W, Zhang Q, Kim Y, Weiss K, Jedrzejczak R, Rosenberg DJ, Fan Y, Wower J, Bierma J, Sarker AH, Tsutakawa SE, Pingali SV, O'Neill HM, Joachimiak A, Hura GL. Biophys J. 2021 Jun 28:S0006-3495(21)00491-4. doi: 10.1016/j.bpj.2021.06.006. PMID: 34197805 

Catalytically impaired TrpA subunit of tryptophan synthase from Chlamydia trachomatis is an allosteric regulator of TrpB. Michalska K, Wellington S, Maltseva N, Jedrzejczak R, Selem-Mojica N, Rosas-Becerra LR, Barona-Gómez F, Hung DT, Joachimiak A. Protein Sci. 2021 Jun 9. doi: 10.1002/pro.4143. PMID: 34107106

Profiling B cell immunodominance after SARS-CoV-2 infection reveals antibody evolution to non-neutralizing viral targets. Dugan HL, Stamper CT, Li L, Changrob S, Asby NW, Halfmann PJ, Zheng NY, Huang M, Shaw DG, Cobb MS, Erickson SA, Guthmiller JJ, Stovicek O, Wang J, Winkler ES, Madariaga ML, Shanmugarajah K, Jansen MO, Amanat F, Stewart I, Utset HA, Huang J, Nelson CA, Dai YN, Hall PD, Jedrzejczak RP, Joachimiak A, Krammer F, Diamond MS, Fremont DH, Kawaoka Y, Wilson PC.Immunity. 2021 Jun 8;54(6):1290-1303.e7. doi: 10.1016/j.immuni.2021.05.001. Epub 2021 May 6.PMID: 34022127

Sensor Domain of Histidine Kinase VxrA of Vibrio cholerae- A Hairpin-swapped Dimer and its Conformational Change. Tan K, Teschler JK, Wu R, Jedrzejczak RP, Zhou M, Shuvalova LA, Endres MJ, Welk LF, Kwon K, Anderson WF, Satchell KJF, Yildiz FH, Joachimiak A.J Bacteriol. 2021 Mar 22:JB.00643-20. doi: 10.1128/JB.00643-20. PMID: 33753465

Distinct B cell subsets give rise to antigen-specific antibody responses against SARS-CoV-2.Wilson P, Stamper C, Dugan H, Li L, Asby N, Halfmann P, Guthmiller J, Zheng NY, Huang M, Stovicek O, Wang J, Madariaga ML, Shanmugarajah K, Jansen M, Amanat F, Stewart I, Changrob S, Utset H, Huang J, Nelson C, Dai YN, Hall P, Jedrzejczak R, Joachimiak A, Krammer F, Fremont D, Kawaoka Y.  Res Sq. 2020 Sep doi: 10.21203/ Preprint. PMID: 32995763

The crystal structure of nsp10-nsp16 heterodimer from SARS-CoV-2 in complex with S-adenosylmethionine.Rosas-Lemus M, Minasov G, Shuvalova L, Inniss NL, Kiryukhina O, Wiersum G, Kim Y, Jedrzejczak R, Maltseva NI, Endres M, Jaroszewski L, Godzik A, Joachimiak A, Satchell KJF. bioRxiv. 2020 Apr 26:2020.04.17.047498. doi: 10.1101/2020.04.17.047498. Preprint. PMID: 32511376



Current Beamline Statistics

APS-U Capabilities with SBC and eBERlight

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 Darren Sherrell (   Recent publication: 2'-O methylation of RNA cap in SARS-CoV-2 captured by serial crystallography.

The 2021 APS/CNM Users Meeting was held virtually during the weeks of May 3-7 and May 10-14, 2021. Please check the links below for meeting program materials and archives.

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)

Virtual APS Tour - Click Here