
NSF Org: |
TI Translational Impacts |
Recipient: |
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Initial Amendment Date: | November 4, 2003 |
Latest Amendment Date: | October 18, 2006 |
Award Number: | 0321581 |
Award Instrument: | Standard Grant |
Program Manager: |
F.C. Thomas Allnutt
TI Translational Impacts TIP Directorate for Technology, Innovation, and Partnerships |
Start Date: | December 1, 2003 |
End Date: | November 30, 2007 (Estimated) |
Total Intended Award Amount: | $0.00 |
Total Awarded Amount to Date: | $749,730.00 |
Funds Obligated to Date: |
FY 2006 = $249,827.00 |
History of Investigator: |
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Recipient Sponsored Research Office: |
15 TECH VALLEY DR STE 1 EAST GREENBUSH NY US 12061-4137 (518)880-1500 |
Sponsor Congressional District: |
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Primary Place of Performance: |
15 TECH VALLEY DR STE 1 EAST GREENBUSH NY US 12061-4137 |
Primary Place of
Performance Congressional District: |
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Unique Entity Identifier (UEI): |
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Parent UEI: |
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NSF Program(s): | SBIR Phase II |
Primary Program Source: |
app-0106 |
Program Reference Code(s): |
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Program Element Code(s): |
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Award Agency Code: | 4900 |
Fund Agency Code: | 4900 |
Assistance Listing Number(s): | 47.084 |
ABSTRACT
This Small Business Innovation Research (SBIR) Phase II project will develop a new convergent x-ray beam based crystallography system for measurement of the quality and the structure of protein crystals in an effort to support crystal growth development efforts and as a prescreening tool for very small protein crystals prior to refined, high-resolution structure determination at dedicated synchrotron-based macromolecular structure facilities. Measurements of a broad range of crystal types, sizes, and degrees of perfection will be carried out in an active protein crystal growth and characterization laboratory at the Wadsworth Center of the New York State Health Department. Parallel measurements using the same crystals will be made in this laboratory with a conventional state-of-the-art protein diffraction system in order to examine the potential benefits and limitations of the convergent beam method (CBM). Measurements will also be made in an industrial laboratory to evaluate the potential of CBM as a commercial, compact, high-intensity, low-power, low-cost, protein screening instrumentation.
The commercial application of this project will be in the area of structural proteomics. Development of a compact, high-efficiency, high-sensitivity system for measurement of the quality and preliminary structure of small protein crystals is crucial to implementation of the huge opportunities offered by recent advances in human and non-human genomics, with far-reaching consequences in the areas of disease therapy and drug discovery. Furthermore, such a system could find broad applications in academic, scientific and industrial programs for high- resolution microscopy of structure, texture, and
strain in metallurgical, geological, environmental and biological or other materials.
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