Crystallization and preliminary crystallographic analysis of the signal recognition particle SRPphi14-9 fusion protein.
The SRPphi14-9 fusion protein, which can functionally replace the SRP9/14 heterodimer in the mammalian signal recognition particle (SRP), has been crystallized using the vapor diffusion method. Four different crystal forms were grown. SRPphi14-9 form IV crystals belong to the space group P4(1)22/ P4(3)22 with cell parameters a = b = 69.7 Angstroms, c = 95.7 Angstroms, alpha = beta = gamma = 90 degrees. A complete data set to 2.8 Angstroms resolution with an Rsym on intensities of 7.0% was collected on a single flash-frozen crystal.
Birse
D E
DE
European Molecular Biology Laboratory, Grenoble Outstation, France.
Doublié
S
S
Kapp
U
U
Strub
K
K
Cusack
S
S
Aberg
A
A
D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D008322:Mammals; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D012645:Selenomethionine / Q000737:chemistry; D018271:Signal Recognition Particle / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D011993:Recombinant Fusion Proteins; D018271:Signal Recognition Particle; D012645:Selenomethionine