title: New results using Laue diffraction and time-resolved crystallography.
abstract: Several time-resolved crystallographic structures were determined over the past year, using a variety of trapping protocols and several data collection methods. A significant theme of recent time-resolved work is the importance of parallel comparative studies on the same protein, using different experimental protocols, in order to fully characterize the structural variation of the intermediates formed in the reaction pathway.
authors.affiliation: Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA. bstoddar@fred.fhcrc.org
authors.forename: B L
authors.initials: BL
authors.lastname: Stoddard
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry; D002374:Catalase / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray / Q000379:methods*; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism; D009195:Peroxidase / Q000737:chemistry / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry / Q000378:metabolism; D020283:Photoreceptors, Microbial; D014367:Tryptophan Synthase / Q000737:chemistry / Q000378:metabolism; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D001426:Bacterial Proteins; D004798:Enzymes; D009211:Myoglobin; D020283:Photoreceptors, Microbial; C050162:photoactive yellow protein, Bacteria; D010088:Oxidoreductases; D002374:Catalase; D009195:Peroxidase; D010744:Phosphoric Monoester Hydrolases; D014367:Tryptophan Synthase