Abstract

The purpose of this project is to provide support to diffraction users (small angle scattering (SAS) and crystallography) and to insure the efficient usage of beam time. This year saw the first regular use Hof beamline X-9B and the sagittal focusing monochromator system to Hperform protein crystallography. This has been spearheaded by Dr. Steve Almo, and the new sub-project abstracts derive from his leadership. The expansion of protein crystallography in general at synchrotrons worldwide is now supported by the X-9B Resource. In the past year, a new MAR (automated image plate) detector has been installed and is in regular use replacing the single FUGI plate system. The support to diffraction users includes personnel support in the form of technical assistance from on site staff on a daily basis such as setting up the x-ray optics, and consultation and/or collaboration with the scientific staff on an arranged basis. In addition, facility support is provided which allows for the construction or purchase of small components which increase either the efficiency of the use of beam time or the flexibility of the experimental set-up.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001633-20
Application #
6618405
Study Section
Project Start
2002-09-01
Project End
2003-08-31
Budget Start
Budget End
Support Year
20
Fiscal Year
2002
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
Dhavan, Gauri M; Crothers, Donald M; Chance, Mark R et al. (2002) Concerted binding and bending of DNA by Escherichia coli integration host factor. J Mol Biol 315:1027-37
Uchida, Takeshi; He, Qin; Ralston, Corie Y et al. (2002) Linkage of monovalent and divalent ion binding in the folding of the P4-P6 domain of the Tetrahymena ribozyme. Biochemistry 41:5799-806
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

Showing the most recent 10 out of 68 publications