Medical College of Wisconsin
Medical College of Wisconsin Cancer Center

Structural Biology Shared Resource (SBSR)

The Structural Biology Shared Resource enables advanced atomic-level studies on the structure and function of cancer related molecules, macromolecules, and their interactions with drugs and biologicals.

Scheduling, Location, and Hours of Operation

Protein Purification Unit: Translational Biomedical Research Center (TBRC), 3rd floor
Cryo-EM facility: Health Research Center, Basement
Monday–Friday from 8 a.m.-5 p.m.
Submit a SBSR iLab Request

Services and Technologies

The SBSR consists of the Protein Purification unit and the Structure Determination unit. The Protein Purification unit produces homogeneous, high-quality proteins well suited for downstream biophysical studies and structure determination. The Structure Determination unit employs X-ray crystallography, Cryo-EM, and advanced AI-assisted analytical tools for structure determination and imaging.

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Cryo-EM

The cryo-EM facility uses a range of high-end user friendly equipment for cryo-imaging of various biological targets. It operates on a fee-for service as well as train and self-use model.

View cryo-EM Instrumentation. (PDF)

Major equipment:

  • Glacios 200 kEV electron microscope
  • MarkIV Vitrobot
  • Pelco EasiGlow
Protein Production

The protein production facility is a fully equipped core for services ranging from cloning to expression of target genes in various cells types including bacteria, insect cells, and mammalian cells. Purified proteins are fully functional for assays and for structure determination. In addition, the facility also had equipment for protein crystallization. The facility routinely produces milligram quantities of purified proteins.

View Protein Production Instrumentation. (PDF)

Major equipment:

  • Agilent Cary Eclipse Spectrophotometer
  • ARI Gryphone Crystallization Robot
  • Bio-Rad NGC Quest 10 Plus FPLC
  • Millipore Guava easyCyte 6-2L HT Cytometer
  • Thermo Scientific Ultimate 3000 UHPLC
  • Incu-Shaker
Structural Biology Shared Resource

iLab Requests; Funding Support

iLab Requests and Support

Funding Support
Investigators should first utilize all available funding resources (below). If funding support is still needed, contact the Shared Resource Director to discuss Cancer Center support.

Researcher at Monitor

Shared Resources Acknowledgement

A condition for using MCW Cancer Center supported Shared Resources is that each Shared Resource is acknowledged in the publication. These acknowledgements enable the Cancer Center to measure and document Shared Resource productivity, impact, and service to members.

View Shared Resource acknowledgment instructions. (PDF)

Leadership

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Wei Liu, PhD

Director, Structural Biology Shared Resource

weiliu@mcw.edu

View Profile

Staff Members

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Ashish Gadicherla, PhD

Interim Technical Director, Assistant Professor

agadicherla@mcw.edu

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Yuanyuan Ma, PharmD

Postdoctoral Researcher

yuma@mcw.edu

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Edwin Legall

Research Technologist

elegall@mcw.edu

Notable Publications

Targeted degradation of GOLM1 by CC-885 via CRL4-CRBN E3 ligase inhibits hepatocellular carcinoma progression. (He J, Guo J, Liu S, Li H, Ma Y, Ma S, Hu Z, Zhao W, Tan M, Liu W, Liu B) Cell Signal 2025 Jun;130:111665 PMID: 39986359; DOI: 10.1016/j.cellsig.2025.111665; Scopus ID: 2-s2.0-85218907304

Structural Insights into Dopamine Receptor-Ligand Interactions: From Agonists to Antagonists. (Barbosa ED, Ma Y, Clift HE, Olson LJ, Zhu L, Liu W) ACS Chem Neurosci 2024 Nov 20;15(22):4123-4131  PMID: 39485723; DOI: 10.1021/acschemneuro.4c00295; Scopus ID: 2-s2.0-85208389275

FOXP4-mediated induction of PTK7 activates the Wnt/β-catenin pathway and promotes ovarian cancer development. (Ji J, Qian Q, Cheng W, Ye X, Jing A, Ma S, Ding Y, Ma X, Wang Y, Sun Q, Wang X, Chen Y, Zhu L, Yuan Q, Xu M, Qin J, Ma L, Yang J, Zhang M, Geng T, Wang S, Wang D, Song Y, Zhang B, Xu Y, Xu L, Liu S, Liu W, Liu B) Cell Death Dis 2024 May 13;15(5):332. PMID: 38740744; PMCID: PMC11091054; DOI: 10.1038/s41419-024-06713-7; Scopus ID: 2-s2.0-85192951272 

CXXC5 drove inflammation and ovarian cancer proliferation via transcriptional activation of ZNF143 and EGR1. (Geng T, Sun Q, He J, Chen Y, Cheng W, Shen J, Liu B, Zhang M, Wang S, Asan K, Song M, Gao Q, Song Y, Liu R, Liu X, Ding Y, Jing A, Ye X, Ren H, Zeng K, Zhou Y, Zhang B, Ma S, Liu W, Liu S, Ji J) Cell Signal 2024 Jul;119:111180. PMID: 38642782; DOI: 10.1016/j.cellsig.2024.111180; Scopus ID: 2-s2.0-85190884720

FBXO5-mediated RNF183 degradation prevents endoplasmic reticulum stress-induced apoptosis and promotes colon cancer progression. (Ji J, Jing A, Ding Y, Ma X, Qian Q, Geng T, Cheng W, Zhang M, Sun Q, Ma S, Wang X, Yuan Q, Xu M, Qin J, Ma L, Yang J, He J, Du Q, Xia M, Xu Y, Chen Z, Zhu L, Liu W, Liu S, Liu B) Cell Death Dis 2024 Jan 11;15(1):33). PMID: 38212299; PMCID: PMC10784456; DOI: 10.1038/s41419-024-06421-2; Scopus ID: 2-s2.0-85182091692 

Structure-Based Lead Optimization of Enterovirus D68 2A Protease Inhibitors. (Tan B, Liu C, Li K, Jadhav P, Lambrinidis G, Zhu L, Olson L, Tan H, Wen Y, Kolocouris A, Liu W, Wang J) J Med Chem 2023 Nov 09;66(21):14544-14563. PMID: 37857371; DOI: 10.1021/acs.jmedchem.3c00995; Scopus ID: 2-s2.0-85176509223

Cryo-EM structure of the human adenosine A2B receptor-Gs signaling complex. (Chen Y, Zhang J, Weng Y, Xu Y, Lu W, Liu W, Liu M, Hua T, Song G) Sci Adv 2022 Dec 23;8(51):eadd3709. PMID: 36563137; PMCID: PMC9788782; DOI: 10.1126/sciadv.add3709; Scopus ID: 2-s2.0-85144637416

An Isochroman Analog of CD3254 and Allyl-, Isochroman-Analogs of NEt-TMN Prove to Be More Potent Retinoid-X-Receptor (RXR) Selective Agonists Than Bexarotene. (Jurutka PW, di Martino O, Reshi S, Mallick S, Sausedo MA, Moen GA, Lee IJ, Ivan DJ, Krall TD, Peoples SJ, Perez A, Tromba L, Le A, Khadka I, Petros R, Savage BM, Salama E, Salama J, Ziller JW, Noh Y, Lee MY, Liu W, Welch JS, Marshall PA, Wagner CE) Int J Mol Sci 2022 Dec 19;23(24). PMID: 36555852; PMCID: PMC9782500; DOI: 10.3390/ijms232416213; Scopus ID: 2-s2.0-85144580245

Structural basis for receptor selectivity and inverse agonism in S1P5 receptors. (Lyapina E, Marin E, Gusach A, Orekhov P, Gerasimov A, Luginina A, Vakhrameev D, Ergasheva M, Kovaleva M, Khusainov G, Khorn P, Shevtsov M, Kovalev K, Bukhdruker S, Okhrimenko I, Popov P, Hu H, Weierstall U, Liu W, Cho Y, Gushchin I, Rogachev A, Bourenkov G, Park S, Park G, Hyun HJ, Park J, Gordeliy V, Borshchevskiy V, Mishin A, Cherezov V) Nat Commun 2022 Aug 12;13(1):4736. PMID: 35961984; PMCID: PMC9374744; DOI: 10.1038/s41467-022-32447-1; Scopus ID: 2-s2.0-85135832975

Structures of β1-adrenergic receptor in complex with Gs and ligands of different efficacies. (Su M, Paknejad N, Zhu L, Wang J, Do HN, Miao Y, Liu W, Hite RK, Huang XY) Nat Commun 2022 Jul 14;13(1):4095. PMID: 35835792; PMCID: PMC9283524; DOI: 10.1038/s41467-022-31823-1; Scopus ID: 2-s2.0-85134147752