Open AccessPurification, crystallization and preliminary X‐ray diffraction of fluorescence recovery protein from Synechocystis PCC 6803
Author(s) -
Liu Ting,
Shuai Yingli,
Zhou Honggang
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911103291x
Subject(s) - crystallization , fluorescence , x ray crystallography , synechocystis , protein crystallization , chemistry , diffraction , crystallography , materials science , biochemistry , optics , physics , organic chemistry , gene , mutant
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 P 4 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 .