Crystallization and preliminary crystallographic analysis of a novel orange fluorescent protein from the Cnidaria tube anemone Cerianthus sp.
A novel orange fluorescent protein, with excitation and emission maxima at 548 and 565 nm, respectively, from the Cnidaria tube anemone Cerianthus sp. has been cloned and overexpressed in Escherichia coli. The orange fluorescent protein has been crystallized by the sitting-drop vapour-diffusion method at 290 K using polyethylene glycol 3350 as a precipitant. A complete set of diffraction data was collected to 2.0 A resolution at 100 K. The crystals belong to the space group R3, with hexagonal unit-cell parameters a = b = 216.947, c = 51.839 A. There are four protein molecules in the asymmetric unit, giving a Matthews coefficient of 2.3 A(3) Da(-1) and a solvent content of 47%.
Ip
Denis T M
DT
Department of Biochemistry, The Chinese University of Hong Kong, Hong Kong SAR, People's Republic of China.
Chan
Siu-Hong
SH
Allen
Mark D
MD
Bycroft
Mark
M
Wan
David C C
DC
Wong
Kam-Bo
KB
D000818:Animals; D003063:Cnidaria / Q000378:metabolism*; D018360:Crystallography, X-Ray / Q000379:methods*; D008164:Luminescent Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D012984:Software
D008164:Luminescent Proteins