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.
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Pfoh, Roland; Pai, Emil F; Saridakis, Vivian (2015) Nicotinamide mononucleotide adenylyltransferase displays alternate binding modes for nicotinamide nucleotides. Acta Crystallogr D Biol Crystallogr 71:2032-9 |
Mariette, Céline; Guérin, Laurent; Rabiller, Philippe et al. (2015) The creation of modulated monoclinic aperiodic composites in n-alkane/urea compounds. Z Kristallogr Cryst Mater 230:5-11 |
Yang, Xiaojing; Stojkovi?, Emina A; Ozarowski, Wesley B et al. (2015) Light Signaling Mechanism of Two Tandem Bacteriophytochromes. Structure 23:1179-89 |
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