The X-ray Crystallography Core facility provides excellent crystallization, data collection, andcrystallographic computing facilities. It also provides outstanding human resources in the form oftalented crystallographers and a strong training environment. Location of the Core facilities adjacent tothe Hill, Sundquist, and Kay labs on the third floor of the EEJMRB provides a convenient and accessibleenvironment that maximizes productive formal and informal interactions. A postdoctoral fellow and astudent within this Core are dedicated to Center projects (VPS4 and ALIX). The two managers andtechnician (50:50 with Bacterial Expression Core) provide expertise and support for additional projects.The core can also support use by other Center personnel and projects as appropriate. For example,Steve Alam (Manager Eukaryotic Protein Expression Core) recently played the lead role ondetermination of the EAP45(ESCRTII) GLUE-ubiquitin crystal structure with assistance from FrankWhitby17; Anna Scott determined the structure of human VPS4B with assistance from Whitby19;Schubert played the lead crystallographic role on the TSG101-ubiquitin complex20, and AndyVanDemark, a postdoc in the Hill lab, recently determined crystal structures of a potent HIV-1 entryinhibitor complex with the gp41 N-peptide (submitted) and a sterically restricted N-peptide antigen (inpreparation) in collaborations with the Kay lab.The strength of the Core is enhanced by interactions with major national facilities and structuralgenomics consortia. Extensive use of remote data collection services (e.g, at NSLS and SSRL) typicallyenables synchrotron data collection within about a week of identifying a suitable crystal. We routinelyutilize the Hauptman-Woodward Institute crystallization facility of the Northeastern Structural GenomicsConsortium. This approach provided initial conditions that led to the preliminary crystals of dodecamericVps4p after vapor diffusion trials failed at our home lab. We recently initiated a novel collaboration withthe Joint Centers for Structural Genomics that will allow the full power of high-throughput methodology tobe applied to the focused scientific questions being addressed by our program. This arrangement willalso allow us to accommodate a potentially high demand for assistance with crystal structuredeterminations by the larger community of HIV biologists, such as through the R21 and othermechanisms.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Specialized Center (P50)
Project #
1P50GM082545-01
Application #
7357381
Study Section
Special Emphasis Panel (ZRG1-AARR-A (40))
Project Start
2007-07-01
Project End
2012-06-30
Budget Start
2007-07-01
Budget End
2008-07-31
Support Year
1
Fiscal Year
2007
Total Cost
$463,783
Indirect Cost
Name
University of Utah
Department
Type
DUNS #
009095365
City
Salt Lake City
State
UT
Country
United States
Zip Code
84112
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Pak, Alexander J; Voth, Gregory A (2018) Advances in coarse-grained modeling of macromolecular complexes. Curr Opin Struct Biol 52:119-126
Redman, Joseph S; Francis, J Nicholas; Marquardt, Robert et al. (2018) Pharmacokinetic and Chemical Synthesis Optimization of a Potent d-Peptide HIV Entry Inhibitor Suitable for Extended-Release Delivery. Mol Pharm 15:1169-1179
Larsen, Kevin P; Mathiharan, Yamuna Kalyani; Kappel, Kalli et al. (2018) Architecture of an HIV-1 reverse transcriptase initiation complex. Nature 557:118-122
Carter, Stephen D; Mageswaran, Shrawan K; Farino, Zachary J et al. (2018) Distinguishing signal from autofluorescence in cryogenic correlated light and electron microscopy of mammalian cells. J Struct Biol 201:15-25
Shepherd, Jason D (2018) Arc - An endogenous neuronal retrovirus? Semin Cell Dev Biol 77:73-78

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