Abstract

The purpose of this project is to provide support to diffraction users (mostly small angle scattering) and to insure the efficient usage of beam time. A major new empahsis for this project is the first regular use of beamline X-9B and the sagittal focusing monochromator system to perform 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. This has, at present, included the fabrication of a FUGI plate setup with rotation stage and cryostream for freezing and stabilization of samples. 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. A general purpose rotation stage has been built which can rotate heavy loads about a vertical or horizontal axis. Among other applications, this will be used for alignment of x-ray crystallography cameras, for steering the beam in the hutch with an x-ray mirror, and for determining the orientation of x-ray monochromator crystals.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001633-14
Application #
5223459
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
14
Fiscal Year
1996
Total Cost
Indirect Cost

  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

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