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Expression, crystallization and preliminary X‐ray diffraction study of FtsY, the docking protein of the signal recognition particle of E. coli
Author(s) -
Montoya Guillermo,
Svensson Cecilia,
Luirink Joen,
Sinning Irmgard
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199706)28:2<285::aid-prot15>3.0.co;2-e
Subject(s) - docking (animal) , crystallization , signal recognition particle , diffraction , crystallography , computational biology , biology , physics , chemistry , optics , biochemistry , signal peptide , peptide sequence , medicine , gene , nursing , thermodynamics
FtsY is the docking protein or SRα homologue in E. coli . It is involved in targeting secretory proteins to the cytoplasmic membrane by interacting with the signal recognition particle, controlled by guanosine 5′‐triphosphate. Two different constructs have been used in crystallization studies: the full‐length protein and a truncated fragment with a his‐tag at the C terminus. Only the second construct resulted in crystals suitable for x‐ray diffraction. The crystals belong to the monoclinic space group P2 1 with cell dimensions a = 32.20 Å, b = 79.57 Å, c = 59.21 Å, and β = 94.45, and contain one molecule per asymmetric unit. At cryogenic temperatures the crystals diffract to a resolution limit of 2.5 Å by using a rotating anode, and beyond 1.8 Å by using synchrotron radiation. Proteins 28:285–288, 1997. © 1997 Wiley‐Liss Inc.