The mission ofthe Protein Structure Laboratory (PSL) is to provide investigators with state-of-the-art instrumentation, facilities, and expertise for all aspects of protein crystallography. This includes protein crystallization. X-ray data collection, data analysis, structure solution and refinement, and structure analysis. Laboratory staff provides advice and consultation, training, access to facilities for experienced crystallographers, and a range of services from crystal growth to structure solution and refinement, and preparation of materials for publications and grant submissions. In addition, the PSL provides training to students, post-docs and faculty who wish to learn any or all aspects of protein structure determination. To facilitate this, modern crystallization methods, in-house or synchrotron X-ray diffraction data collection, and the most recent crystallographic software are utilized. The staff consists of one experienced full time Ph.D. crystallographer. Dr. Scott Lovell, who serves as the Director ofthe Laboratory, and a Research Assistant to assist with crystallization screening and sample preparation for X-ray diffraction experiments. The PSL is located in close proximity to other core service laboratories in the University of Kansas Structural Biology Center building. During Phase II, the PSL has collaborated with 36 investigators from academic, government and industrial institutions. This has resulted in more than 100 structures delivered, 64 deposited to the Protein Databank, 26 publications and 17 grant applications submitted in which the PSL staff were listed. The PSL will continue to expand the base of collaborators and provide high-level facilities, expertise and training during Phase III ofthe COBRE-PSF.

Public Health Relevance

The Protein Structure Core Laboratory uses X-ray crystallography to determine detailed 3-dimensional structures of proteins for investigators. It also provides training in all relevant methods used in protein crystallography.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Center Core Grants (P30)
Project #
1P30GM110761-01
Application #
8735421
Study Section
Special Emphasis Panel (ZGM1-TWD-C (C3))
Project Start
Project End
Budget Start
2014-08-01
Budget End
2015-06-30
Support Year
1
Fiscal Year
2014
Total Cost
$225,000
Indirect Cost
$75,000
Name
University of Kansas Lawrence
Department
Type
DUNS #
076248616
City
Lawrence
State
KS
Country
United States
Zip Code
66045
Wahome, Newton; Sully, Erin; Singer, Christopher et al. (2016) Novel Ricin Subunit Antigens With Enhanced Capacity to Elicit Toxin-Neutralizing Antibody Responses in Mice. J Pharm Sci 105:1603-13
Weerawarna, Pathum M; Kim, Yunjeong; Galasiti Kankanamalage, Anushka C et al. (2016) Structure-based design and synthesis of triazole-based macrocyclic inhibitors of norovirus protease: Structural, biochemical, spectroscopic, and antiviral studies. Eur J Med Chem 119:300-18
Wahome, Newton; Cooper, Anne; Thapa, Prem et al. (2016) Production of Well-Characterized Virus-like Particles in an Escherichia coli-Based Expression Platform for Preclinical Vaccine Assessments. Methods Mol Biol 1404:437-57
Jia, Kaimin; Cao, Ruikai; Hua, Duy H et al. (2016) Study of Class I and Class III Polyhydroxyalkanoate (PHA) Synthases with Substrates Containing a Modified Side Chain. Biomacromolecules 17:1477-85
McShan, Andrew C; Anbanandam, Asokan; Patnaik, Sikta et al. (2016) Characterization of the Binding of Hydroxyindole, Indoleacetic acid, and Morpholinoaniline to the Salmonella Type III Secretion System Proteins SipD and SipB. ChemMedChem 11:963-71
Gowthaman, Ragul; Miller, Sven A; Rogers, Steven et al. (2016) DARC: Mapping Surface Topography by Ray-Casting for Effective Virtual Screening at Protein Interaction Sites. J Med Chem 59:4152-70
Budiardjo, S Jimmy; Licknack, Timothy J; Cory, Michael B et al. (2016) Full and Partial Agonism of a Designed Enzyme Switch. ACS Synth Biol 5:1475-1484
Tifrea, Delia F; Barta, Michael L; Pal, Sukumar et al. (2016) Computational modeling of TC0583 as a putative component of the Chlamydia muridarum V-type ATP synthase complex and assessment of its protective capabilities as a vaccine antigen. Microbes Infect 18:245-53
Kaur, Kawaljit; Chatterjee, Srirupa; De Guzman, Roberto N (2016) Characterization of the Shigella and Salmonella Type III Secretion System Tip-Translocon Protein-Protein Interaction by Paramagnetic Relaxation Enhancement. Chembiochem 17:745-52
O'Neil, Pierce; Lovell, Scott; Mehzabeen, Nurjahan et al. (2016) Crystal structure of histone-like protein from Streptococcus mutans refined to 1.9 Å resolution. Acta Crystallogr F Struct Biol Commun 72:257-62

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