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

FEBS Letters

Brown, Kieron¹  Kapp, Ulrike¹  Cusack, Stephen¹  Åberg, Anders¹  Doublié, Sylvie¹  Strub, Katharina² 

[1] European Molecular Biology Laboratory Grenoble Outstation, c/o ILL, BP 156X, 38042 Grenoble Cédex, France;Département de Biologie Cellulaire, Université de Genève, Sciences III, CH-1211 Geneva 4, Switzerland

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;   

DOI  :  10.1016/0014-5793(96)00316-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown