The purpose of this project is to provide support to spectroscopy users and to insure the efficient usage of beam time. This includes personnel support in the form of technical assistance from on site staff on a daily basis, and consultation and/or collaboration with the Director (Dr. Chance) on a weekly basis. The improvements to the sagittally focusing monochromator described in the X9B Performance and Upgrades Abstract, have led to direct improvements in the quality of XAS data recorded at X9B. Also, it has led to XAS users utilizing the focusing crystals (as opposed to the flat crystal set) 66% of the time currently. The use of a focused beam results in a smaller beam size at the specimen. Vacuum beam transport tubes have been used resulting in more of the X-ray beam being delivered to the specimen and less of the beam scattering elastically off the sample holder: thus the ratio of the fluorescence X-ray signal to elastically scattered background has been improved. The increased flux delivered with the sagittally focusing monochromator allows one to increase the specimen to detector distance and further increases the signal to background ratio. (The outer elements of the 13-element Ge-detector view the specimen at closer to 90 degrees relative to the incident beam where the elastically scattered flux is a minimum.) Because of the improved data quality and the transparency of usage of the dynamically focused beam most of the XAS users now collect data in this mode. Additionally, the smaller beam sizes at the specimen means smaller quantities of precious materials are required.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001633-14
Application #
5223458
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
14
Fiscal Year
1996
Total Cost
Indirect Cost
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