CRYSTALLOGRAPHIC ANALYSES OF (MOSTLY) METALLOPROTEINS AND MEMBRANE PROTEINS

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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. We wish to collect x-ray diffraction data from crystals of membrane proteins that mediate the passage of molecules, electrons and information across the membrane bilayer. We have previously determined the structure of the gated mechanosensitive channel of large conductance (MscL) from Mycobacterium tuberculosis, a prokaryotic channel that functions as an osmotic pressure safety valve (Chang et al. Science 282, 2220 (1998)), and the structure of fumarate reductase (FRD) that catalyzes the final step of anaerobic respiration when fumarate is the terminal electron acceptor (Iverson et al., Science 284, 1961 (1999)). Building upon this foundation, we have crystallized two new membrane protein systems, MscS and an ABC transporter, that achieve the transmembrane passage of molecules. The high intensity crystallography beamlines at SSRL will be essential for native data collection, for the use of MAD phasing methods in the structure determinations, and to identify ligand binding sites on these proteins.