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

Publications Highlights

Fixed-target serial crystallography at the Structural Biology Center. Sherrell DA, Lavens A, Wilamowski M, Kim Y, Chard R, Lazarski K, Rosenbaum G, Vescovi R, Johnson JL, Akins C, Chang C, Michalska K, Babnigg G, Foster I, Joachimiak A.J Synchrotron Radiat. 2022 Sep 1;29(Pt 5):1141-1151. doi: 10.1107/S1600577522007895. Epub 2022 Aug 17.PMID: 36073872

Proteolytic processing induces a conformational switch required for antibacterial toxin delivery. Bartelli NL, Passanisi VJ, Michalska K, Song K, Nhan DQ, Zhou H, Cuthbert BJ, Stols LM, Eschenfeldt WH, Wilson NG, Basra JS, Cortes R, Noorsher Z, Gabraiel Y, Poonen-Honig I, Seacord EC, Goulding CW, Low DA, Joachimiak A, Dahlquist FW, Hayes CS.Nat Commun. 2022 Aug 29;13(1):5078. doi: 10.1038/s41467-022-32795-y.PMID: 36038560 

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 21:rs.3.rs-1840200. doi: 10.21203/rs.3.rs-1840200/v1. Preprint.PMID: 35898342 

The first crystal structure of a xylobiose-bound xylobiohydrolase with high functional specificity from the bacterial glycoside hydrolase family 30, subfamily 10. St John FJ, Crooks C, Kim Y, Tan K, Joachimiak A.FEBS Lett. 2022 Sep;596(18):2449-2464. doi: 10.1002/1873-3468.14454. Epub 2022 Aug 4.PMID: 35876256

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

 
Publications
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Current Beamline Statistics
Announcements

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 eBERlight@anl.gov.

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 (kmichalska@anl.gov).   Recent publication: 2'-O methylation of RNA cap in SARS-CoV-2 captured by serial crystallography.

The APS will pause user experiments on April 17, 2023.  The APS is installing a new storage ring that will require a year-long shutdown period.  More information on the APS-U:  https://www.aps.anl.gov/APS-Upgrade

The APCF will be open for users during the APS-U shutdown. 
Submit an ESAF for Sector 84.

The 2023 APS/CNM Users Meeting will take place April 17-21, 2023.
Meeting agenda and registration coming soon.

APS Overview Virtual Tour