title: High-temperature and high-resolution crystallography of thermostable copper nitrite reductase.
abstract: The 1.55 Å resolution thermostable copper nitrite reductase structure at 320 K displayed a near-bidentate binding mode of nitrite distinct from a monodentate mode in a cryogenic structure. To our knowledge, this is the first case in which the difference in substrate binding modes between cryogenic and high-temperature structures has been visualized by crystallography.
authors.affiliation: Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan. y_fukuda@chem.eng.osaka-u.ac.jp.
authors.forename: Yohta
authors.initials: Y
authors.lastname: Fukuda
authors.forename: Tsuyoshi
authors.initials: T
authors.lastname: Inoue
mesh_terms: D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D008958:Models, Molecular; D009572:Nitrite Reductases / Q000737:chemistry*; D011487:Protein Conformation; D013696:Temperature
chemical_list: D009572:Nitrite Reductases; C052695:nitrite reductase, copper-containing