Crystallization and preliminary crystallographic analysis of the signal recognition particle SRPΦ14‐9 fusion protein

[摘要]

The SRPΦ14-9 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. SRPΦ14-9 form IV crystals belong to the space group P4₁22/P4₃22 with cell parameters . A complete data set to 2.8 Å resolution with an R _sym on intensities of 7.0% was collected on a single flashfrozen crystal.

[学科分类] 生物化学/生物物理

[关键词] Signal recognition particle (SRP);Fusion protein;Purification;Crystal;X-ray diffraction;Synchrotron;BICINE;N;N-bis[2-hydroxyethyl]glycine hydrochloride;CAPS;3-[cyclohexylamino]-1-propanesulfonic acid;EDTA;N;N′-1;2-ethanediylbis[N-(carboxymethyl]glycine;EMBL;European Molecular Biology Laboratory;ESRF;European Synchrotron Radiation Facility;HEPES;N-[2-hydroxyethyl]piperazine-N′-[2′-ethanesulfonic acid];IPTG;isopropyl-β-d-thiogalactopyranoside;MES;2-[N-morpholino]ethanesulfonic acid;MPD;2-methyl-2;4-pentanediol;PAGE;polyacrylamide gel electrophoresis;PEG;polyethylene glycol;PMSF;phenylmethylsulfonyl fluoride;RER;rough endoplasmic reticulum;SDS;sodium dodecyl sulfate;SRP;signal recognition particle;SRP9/14;signal recognition particle proteins SRP9 and SRP14 heterodimer;SRPΦ14-9;SRP9/14 fusion protein;TRIS;tris[hydroxymethyl]aminomethane hydrochloride