title: Purification, crystallization and preliminary X-ray diffraction of fluorescence recovery protein from Synechocystis PCC 6803.
abstract: Fluorescence recovery protein (FRP), which is encoded by the slr1964 gene in Synechocystis PCC 6803, plays a key role in the orange carotenoid protein-related photoprotective mechanism in cyanobacteria. As the crystal structure of FRP may provide information about the biological functions and mechanism of action of the protein, recombinant full-length FRP and a truncated form were overexpressed, purified and crystallized at 291 K using ethylene imine polymer as the precipitant. An FRP data set was collected to a resolution of 2.75 Å at low temperature (100 K). The crystal belonged to space group P4(1)2(1)2, with unit-cell parameters a = b = 61.9, c = 160.7 Å, α = β = γ = 90°. Assuming that the asymmetric unit contains three molecules, the Matthews coefficient was calculated to be 2.1 Å(3) Da(-1).
authors.affiliation: College of Life Sciences and Tianjin State Laboratory of Protein Science, Nankai University, Tianjin, People's Republic of China.
authors.forename: Ting
authors.initials: T
authors.lastname: Liu
authors.forename: Yingli
authors.initials: Y
authors.lastname: Shuai
authors.forename: Honggang
authors.initials: H
authors.lastname: Zhou
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D046939:Synechocystis / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins