Abstract

This project has successfully sought funding from the NSF Biological Instrumentation program for the completion of a state of the art, bending magnet, protein crystallography station on the X9A beamline of the National Synchrotron Light Source (NSLS) at Brookhaven National Laboratories. The plan includes the purchase of the beamline optical components (i.e., monochromator and mirror) as well as a CCD detector and associated automation and computing hardware for rapid and efficient data collection and reduction. This facility will provide the crystallographic communities at the Albert Einstein College of Medicine (AECOM), Rockefeller University (RU) and the Sloan-Kettering Institute (SKI) with 170 days of access per year to high flux, tunable synchrotron radiation, and will allow for rapid progress on existing projects, as well as the initiation and timely completion of new structural problems. In addition, this facility will provide 60 days of beam time to the protein crystallography community nationwide through the NSLS General User program, which requires that at least 25% of the total beam time be distributed through a peer reviewed process administered by NSLS.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001633-18
Application #
6345151
Study Section
Project Start
2000-09-01
Project End
2001-08-31
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
18
Fiscal Year
2000
Total Cost
Indirect Cost

  Institution

Name
Albert Einstein College of Medicine
Department
Type
DUNS #
009095365
City
Bronx
State
NY
Country
United States
Zip Code
10461

  Publications

Vongsvivut, Jitraporn; Fernandez, Jason; Ekgasit, Sanong et al. (2004) Characterization of supported cylinder-planar germanium waveguide sensors with synchrotron infrared radiation. Appl Spectrosc 58:143-51
Masip, Lluis; Pan, Jonathan L; Haldar, Suranjana et al. (2004) An engineered pathway for the formation of protein disulfide bonds. Science 303:1185-9
Huang, Raymond Y; Miller, Lisa M; Carlson, Cathy S et al. (2003) In situ chemistry of osteoporosis revealed by synchrotron infrared microspectroscopy. Bone 33:514-21
Rashidzadeh, Hassan; Khrapunov, Sergei; Chance, Mark R et al. (2003) Solution structure and interdomain interactions of the Saccharomyces cerevisiae ""TATA binding protein"" (TBP) probed by radiolytic protein footprinting. Biochemistry 42:3655-65
Uchida, Takeshi; Takamoto, Keiji; He, Qin et al. (2003) Multiple monovalent ion-dependent pathways for the folding of the L-21 Tetrahymena thermophila ribozyme. J Mol Biol 328:463-78
Taylor, Colleen M; Watton, Stephen P; Bryngelson, Peter A et al. (2003) Inner-sphere complexation of cobalt(II) 2,9-dimethyl-1,10-phenanthroline ([Co(neo)]2+) with commercial and sol-gel derived silica gel surfaces. Inorg Chem 42:312-20
Tang, Qun; Carrington, Paul E; Horng, Yih-Chern et al. (2002) X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation. J Am Chem Soc 124:13242-56
Guan, Jing-Qu; Vorobiev, Sergeui; Almo, Steven C et al. (2002) Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting. Biochemistry 41:5765-75
Chance, Mark R; Bresnick, Anne R; Burley, Stephen K et al. (2002) Structural genomics: a pipeline for providing structures for the biologist. Protein Sci 11:723-38
Maleknia, Simin D; Kiselar, Janna G; Downard, Kevin M (2002) Hydroxyl radical probe of the surface of lysozyme by synchrotron radiolysis and mass spectrometry. Rapid Commun Mass Spectrom 16:53-61

Showing the most recent 10 out of 68 publications