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Grazing‐angle characterization of photosynthetic oxygen evolution protein monolayers
dc.contributor.authorYu, Eileen Y.en_US
dc.contributor.authorPenner‐hahn, James E.en_US
dc.contributor.authorYocum, Charles F.en_US
dc.contributor.authorMayer, Robert H.en_US
dc.contributor.authorPickering, Ingrid J.en_US
dc.date.accessioned2010-05-06T22:50:18Z
dc.date.available2010-05-06T22:50:18Z
dc.date.issued1996-09en_US
dc.identifier.citationYu, Eileen Y.; Penner‐Hahn, James E.; Yocum, Charles F.; Mayer, Robert H.; Pickering, Ingrid J. (1996). "Grazing‐angle characterization of photosynthetic oxygen evolution protein monolayers." Review of Scientific Instruments 67(9): 3364-3364. <http://hdl.handle.net/2027.42/70867>en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/70867
dc.description.abstractVariable‐period x‐ray standing wave (XSW) spectroscopy has been shown to be a practical probe for studying metalloproteins. The photosynthetic oxygen evolving complex (OEC) is a transmembrane multipolypeptide complex that catalyzes the oxidation of water to dioxygen. The OEC contains Mn, Ca, and Cl and is potentially amenable to study by XSW. In this feasibility study, preliminary results on OEC samples deposited on Au mirrors are discussed. First XSW measurements from the SSRL grazing‐incidence setup are presented. © 1996 American Institute of Physics.en_US
dc.format.extent3102 bytes
dc.format.extent779233 bytes
dc.format.mimetypetext/plain
dc.format.mimetypeapplication/pdf
dc.publisherThe American Institute of Physicsen_US
dc.rights© The American Institute of Physicsen_US
dc.titleGrazing‐angle characterization of photosynthetic oxygen evolution protein monolayersen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelPhysicsen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumBiophysics Research Division, University of Michigan, Ann Arbor, MI 48109en_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109en_US
dc.contributor.affiliationumDepartment of Biology, University of Michigan, Ann Arbor, MI 48109en_US
dc.contributor.affiliationotherStanford Synchrotron Radiation Laboratory, Stanford, CA 94309en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/70867/2/RSINAK-67-9-3364-5.pdf
dc.identifier.doi10.1063/1.1147356en_US
dc.identifier.sourceReview of Scientific Instrumentsen_US
dc.owningcollnamePhysics, Department of


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