Crystallization and preliminary X‐ray analysis of the 9 kDa protein of the mouse signal recognition particle and the selenomethionyl‐SRP9

[摘要]

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 × 0.1 × 0.1 mm³ and they diffract to a resolution of 2.3 Å. They belong to the space groups P6₂22/P6₄22 or P3₁21/P3₂21 with cell dimensions . Crystals have also been grown from the selenomethionyl protein and multiwavelength data sets have been collected.

[学科分类] 生物化学/生物物理

[关键词] Signal recognition particle;Incomplete factorial design;Selenomethionyl protein;Crystallization;X-ray diffraction;EDTA;N;N′-1;2-ethanediylbis[N-(carboxymethyl)glycine;ESRF;European Synchrotron Radiation Facility;EMBL;European Molecular Biology Laboratory;IPTG;isopropyl-β-d-thiogalactopyranoside;MES;2-[N-Morpholino]ethanesulphonic acid;PEG;polyethylene glycol;REP;rough endoplasmic reticulum;SRP;signal recognition particle;SRP9/14;signal recognition particle proteins SRP9 and SRP14 heterodimer;SRPΦ14-9;SRP9/14 fusion protein;Tris-HCl;Tris[hydroxymethyl]aminomethane hydrochloride