Abstract

To provide dedicated access to footprinting technology, beamline X9A at the National Synchrotron Light Source is maintained along with a dedicated stopped flow instrument to allow footprinting studies for our expanded group of investigators. The beamline accepts up to 5 milliradians of white beam, with a flux density of 109 photons/s/mm2/0.07% bandwidth over an effective energy range of 3-30 keV. A dedicated beamline is necessary for high productivity of the core and collaborative research project. Our Resource is the world leader in this technology and the availability of a dedicated beamline will continue our leadership in this area. We are now routinely conducting footprinting studies on 5-10 msec and longer timescales with our stopped flow device. Major advances in understanding RNA folding have been accomplished and studies of protein-DNA complex formation have been initiated. The dedicated footprinting beamline will be moved to a new station (X28C) in late 1999 to make way for the new crystallography program at X9A. The resource has been given access to the new beamline by the NSLS.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001633-19
Application #
6491430
Study Section
Project Start
2001-09-01
Project End
2002-08-31
Budget Start
Budget End
Support Year
19
Fiscal Year
2001
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
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
Marinkovic, N S; Huang, R; Bromberg, P et al. (2002) Center for Synchrotron Biosciences' U2B beamline: an international resource for biological infrared spectroscopy. J Synchrotron Radiat 9:189-97
Huang, R Y; Miller, L M; Carlson, C S et al. (2002) Characterization of bone mineral composition in the proximal tibia of cynomolgus monkeys: effect of ovariectomy and nandrolone decanoate treatment. Bone 30:492-7

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