Crystallization and preliminary X-ray diffraction analysis of the red fluorescent protein eqFP611.
A novel red fluorescent protein, eqFP611, from the sea anemone Entacmaea quadricolor has been cloned in Escherichia coli. With excitation and emission maxima at 559 and 611 nm, this protein shows the most red-shifted emission and the largest Stokes shift of all non-modified proteins in the green fluorescent protein (GFP) family. The protein fluoresces over a wide pH range (4-10) with high quantum yield (0.45). Its photophysical properties make eqFP611 an excellent marker protein for in vivo labeling in eukaryotic systems as was shown by expression in a mammalian cell culture. eqFP611 has been crystallized in space group P6(5)22, with unit-cell parameters a = b = 77.26, c = 329.49 A. The unit cell contains 12 asymmetric units, with two monomers in each. A molecular-replacement solution has been obtained using the 48.4% homologous red fluorescent protein from Discosoma coral (DsRed).
Nienhaus
Karin
K
Department of Biophysics, University of Ulm, 89069 Ulm, Germany.
Vallone
Beatrice
B
Renzi
Fabiana
F
Wiedenmann
Jörg
J
Nienhaus
G Ulrich
GU
D000818:Animals; D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D004926:Escherichia coli / Q000235:genetics; D015723:Gene Library; D008164:Luminescent Proteins / Q000737:chemistry*; D012615:Sea Anemones / Q000737:chemistry*; D014961:X-Ray Diffraction / Q000379:methods; D000097573:Red Fluorescent Protein
D008164:Luminescent Proteins; D000097573:Red Fluorescent Protein