title: Purification, crystallization and preliminary X-ray crystallographic analysis of the lumenal domain of the ER-vesicle protein Erv41p from Saccharomyces cerevisiae.
abstract: The membrane protein Erv41p is a major component of COPII-coated vesicles and is thought to play a role in the early secretory pathway in eukaryotic cells. In this study, the full lumenal domain of Erv41p from Saccharomyces cerevisiae (ScErv41p_LD) was recombinantly expressed in Sf9 insect cells and purified by nickel-affinity, ion-exchange and size-exclusion chromatography. ScErv41p_LD crystals were obtained using the sitting-drop vapour-diffusion method and native X-ray diffraction data were collected to 2.0 Å resolution. The crystals belonged to space group P21, with unit-cell parameters a = 49.8, b = 76.9, c = 65.1 Å, α = γ = 90.0, β = 104.8°.
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Tomtebodavägen 6, S171-77 Stockholm, Sweden.
authors.forename: Ekaterina I
authors.initials: EI
authors.lastname: Biterova
authors.forename: Maria
authors.initials: M
authors.lastname: Svärd
authors.forename: Dominik D D
authors.initials: DD
authors.lastname: Possner
authors.forename: Jodie E
authors.initials: JE
authors.lastname: Guy
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004721:Endoplasmic Reticulum / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D014961:X-Ray Diffraction
chemical_list: C469738:Erv41 protein, S cerevisiae; D008565:Membrane Proteins; D029701:Saccharomyces cerevisiae Proteins
keywords: COPII; Erv proteins; Erv41p; Saccharomyces cerevisiae