Cloning, expression, crystallization and preliminary X-ray analysis of the first two Ig domains from human Roundabout 1 (Robo1)

Autor: Morlot, C., Hemrika, W., Romijn, R.A., Gros, P., Cusack, S., McCarthy, A.A., Kristal- en structuurchemie, Dep Scheikunde
Rok vydání: 2007
Zdroj: Acta crystallographica. Section F, Structural biology and crystallization communications, F63, 689. Wiley-Blackwell
ISSN: 1744-3091
Popis: Activation of Roundabout 1 (Robo1) by Slit proteins results in axon repulsion from the midline. Robo1 is a large transmembrane receptor expressed on the axon growth cone and the minimal Robo1-binding region required for Slit activation has been mapped to the N-terminal Ig1-2 domains. The cDNA encoding the first two Ig domains of Robo1 has been cloned and the protein has been expressed in HEK293 EBNA-1 mammalian cells. Here, the purification and crystallization conditions of this Robo1 construct are reported. The crystals are orthorhombic, space group P21212, with unit-cell parameters a = 38.8, b = 69.4, c = 103.3 Å and one molecule in the asymmetric unit. X-ray diffraction data have been collected to 2.8 Å resolution on beamline ID29 at the ESRF.
Databáze: OpenAIRE