Crystallization and preliminary X-ray analysis of the 9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9.
Two different crystal forms of the 9 kDa protein of the signal recognition particle (SRP9) have been prepared by the hanging drop vapor diffusion technique using 28% (w/v) PEG8000 or 28% saturated ammonium sulphate as precipitant. The crystals are hexagonal bipyramids with average dimensions of 0.2 X 0.1 X 0.1 mm(3) and they diffract to a resolution of 2.3 Angstroms. They belong to the space groups P6(2)22/P6(4)22 or P3(1)21/P3(2)21 with cell dimensions a = b = 63.0 Angstroms, and c = 111.5 Angstroms. Crystals have also been grown from the selenomethionyl protein and multiwavelength data sets have been collected.
Doublié
S
S
European Molecular Biology Laboratory, Grenoble Outstation, France.
Kapp
U
U
Aberg
A
A
Brown
K
K
Strub
K
K
Cusack
S
S
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000295:instrumentation / Q000379:methods; D004058:Diffusion; D051379:Mice; D012645:Selenomethionine / Q000737:chemistry*; D018271:Signal Recognition Particle / Q000737:chemistry*
D018271:Signal Recognition Particle; C503637:Srp72 protein, mouse; D012645:Selenomethionine