HIGH RESOLUTION STRUCTURAL STUDIES ON MACROMOLECULAR CRYSTALS

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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. Synchrotron X-ray diffraction data will be collected for seven different crystallographic projects. (1) A mutant glucose isomerase system, substrate free, substrate bound and active site will be investigated to obtain ultra-high resolution structures. This effort will be coordinated with a neutron diffraction study on all three samples scheduled for beamtime at the Institute Laue Langevin in November 2001 in which we will elucidate the enzymatic mechanism. (2) Medium resolution synchrotron data (>3 ¿¿ will be collected on a bFGF/DNA complex that has thus far eluded laboratory studies due to the large unit cell edge. (3) A MAD study will be carried out to obtain the structure of the C1, titin 2-domain fragment, (4) Equine serum albumin will be used for studying the effects of microgravity and to improve the resolution of the current structure. (5) Finally structural studies will be carried out on Der f2, a dust mite allergen (6) on an RNA dodecamer, and (7) on RNA pseudoknot. Each system has industrial, biomedical and in the case of the equine serum albumin study, fundamental importance.