Abstract

The NSLS, in collaboration with SPring-8, Japan, has designed, built and tested a prototype ?small-gap? undulator, whose compactness allows it to reside between the rf cavities that exist at X9 and X29. This prototype in-vacuum undulator (IVUN), with a period of 11 mm, a minimum useful gap of 3.3 mm (maximum of 10 mm) and a magnetic field of 0.678 T is currently installed in the straight section for beamline X13. These parameters lead to a measured fundamental at 4.6 keV, second harmonic at 8.7 keV, and a third harmonic at 13.9 keV. The brightness of IVUN is comparable (slightly higher) than the X25 wiggler. Since its brightness is significantly less than that of the APS devices, the corollary is that the spectral width is greater, in fact sufficient to perform a MAD experiment around selected absorption edges if the peak energy is carefully selected. The X13 undulator will provide the basis for the design and construction of a completely dedicated small-gap undulator station for MAD data collection at the Se edge at NSLS. The availability of such a facility will greatly increase the total number of MAD days available to the scientific community and will serve as a model for the further development and implementation of small-gap undulators as major resources in structural, molecular and cellular biology.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001633-19
Application #
6491510
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

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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
Dewan, John C; Feeling-Taylor, Angela; Puius, Yoram A et al. (2002) Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A resolution. Acta Crystallogr D Biol Crystallogr 58:2038-42
Kiselar, J G; Maleknia, S D; Sullivan, M et al. (2002) Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry. Int J Radiat Biol 78:101-14
Swisher, Jennifer F; Su, Linhui J; Brenowitz, Michael et al. (2002) Productive folding to the native state by a group II intron ribozyme. J Mol Biol 315:297-310
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

Showing the most recent 10 out of 68 publications