Expression, crystallization and preliminary X-ray diffraction study of FtsY, the docking protein of the signal recognition particle of E. coli

✍ Scribed by Guillermo Montoya; Cecilia Svensson; Joen Luirink; Irmgard Sinning

• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 47 KB
• Volume: 28
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/(sici)1097-0134(199706)28:2<285::aid-prot15>3.0.co;2-e

✦ Synopsis

FtsY is the docking protein or SRa 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 58-triphosphate. Two different constructs have been used in crystallization studies: the fulllength 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 5 32.20 Å, b 5 79.57 Å, c 5 59.21 Å, and b 5 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.