Structural Biology & Biophysics Facility
Overview
The Structural Biology and Biophysics Facility is a University of Rochester research resource located within the Department of Biochemistry & Biophysics. Our goal is to provide non-specialist and specialist users with access to biophysical instrumentation designed to:
- Determine macromolecular structures by X-ray crystallography
- Quantitatively characterize biomolecular interactions
The facility features the following equipment:
- Bruker AXS X8 Prospector Ultra microfocus IµS sealed-tube X-ray generator
- Mosquito crystallization robot (TTP LabTech) or high-throughput, nanoliter-scale crystallization experiments
- Microscopes for crystal viewing
- Computers and software for structure determination and graphics
- Dynamic Light Scattering (DLS) DynaPro Plate Reader II (Wyatt Technologies)
- BIAcore T200 for automated surface plasmon resonance (SPR)
- VP-ITC (Microcal) isothermal titration calorimeter
- Fluoromax-3 fluorimeter
Staff
Dr. Jermaine Jenkins is the Facility Manager who is available to train individuals in the use of core instruments. He can also assist with experimental design and data interpretation. Dr. Jenkins reports to the Executive Directors of the facility, Profs. Joseph Wedekind and Clara Kielkopf. Operation of the Facility is overseen by a steering committee comprised of local scientists.
Publications resulting from the use of instrumentation should reference support from NIH NCRR grants 1S10 RR026501 and 1S10 RR027241, as well as NIH NIAID P30 AI078498 and the University of Rochester SMD.
Recent Facility Publications
Liberman JA, Salim M, Krucinska J, Wedekind JE (2013). Structure of a class II preQ1 riboswitch reveals ligand recognition by a new fold. Nature Chem. Biol. 10.1038/NChemBio.1231.
Gleghorn ML, Gong C, Kielkopf CL, Maquat LE (2013). Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRNA decay. Nat Struct Mol Biol. 20, 515-24.
Jenkins JL, Agrawal AA, Gupta A, Green MR, Kielkopf CL (2013). U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs. Nucleic Acids Res. 41, 3859-73.
Wang W, Maucuer A, Gupta A, Manceau V, Thickman KR, Bauer WJ, Kennedy SD, Wedekind JE, Green MR, Kielkopf CL (2013). Structure of phosphorylated SF1 bound to U2AF65 in an essential splicing factor complex. Structure 21, 197-208.
