This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The proposed research will involve screening and high resolution native data collection and MIR and MAD data collection on heavy metal derivatized crystals for phasing and structure determination of proteins that have been recombinantly expressed in E.coli and baculovirus systems. The proteins targeted include enzymes from the proteome of SARS virus, those involved in protein-protein interactions, enzymes with novel folds and functions and those considered tough structure targets e.g., those with putative transmembrane domains, Fatty acid amide hydrolase and the light chain complex. The data collection protocols will be those used routinely like MAD and MIR experiments from Selenomethionine derivatized crystals and/or native crystals soaked with different heavy atoms for phasing. All proteins are crystallized after being recombinantly expressed in either E.coli or Baculovirus and purified by metal affinity, ion exchange and size-exclusion and are NOT considered a biohazard.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR007707-15
Application #
7366184
Study Section
Special Emphasis Panel (ZRG1-BBCB (01))
Project Start
2006-08-01
Project End
2007-07-31
Budget Start
2006-08-01
Budget End
2007-07-31
Support Year
15
Fiscal Year
2006
Total Cost
$43,246
Indirect Cost
Name
University of Chicago
Department
Biochemistry
Type
Schools of Medicine
DUNS #
005421136
City
Chicago
State
IL
Country
United States
Zip Code
60637
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Yang, Cheolhee; Choi, Minseo; Kim, Jong Goo et al. (2018) Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering. Int J Mol Sci 19:
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