title: Spectroscopic characterization of bacteriorhodopsin's L-intermediate in 3D crystals cooled to 170 K.
abstract: Spectra are presented from a single 3D microcrystal of bacteriorhodopsin (bR) cooled to 170 K under various illumination conditions. This set is necessary and sufficient to assign the relevant crystal reference spectra. A spectral decomposition of the difference spectrum obtained following the trapping protocol of Royant et al. (2000) (Nature 406, 645-648) is given, confirming that the low temperature L-intermediate was the species that dominated the structural rearrangements previously reported. Smaller contributions from the K and M spectral intermediates are also quantified. Mechanistic insights derived from the X-ray structures of the early bR intermediates are discussed.
authors.affiliation: Institut de Biologie Structurale, UMR 5075-CEA-CNRS-Université Joseph Fourier, Grenoble, France.
authors.forename: A
authors.initials: A
authors.lastname: Royant
authors.forename: K
authors.initials: K
authors.lastname: Edman
authors.forename: T
authors.initials: T
authors.lastname: Ursby
authors.forename: E
authors.initials: E
authors.lastname: Pebay-Peyroula
authors.forename: E M
authors.initials: EM
authors.lastname: Landau
authors.forename: R
authors.initials: R
authors.lastname: Neutze
mesh_terms: D001436:Bacteriorhodopsins / Q000737:chemistry* / Q000528:radiation effects; D003080:Cold Temperature; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D010777:Photochemistry; D013053:Spectrophotometry; D055672:Static Electricity
chemical_list: D001436:Bacteriorhodopsins