title: Purification, crystallization and preliminary crystallographic studies of the ligand-binding domain of a plant vacuolar sorting receptor.
abstract: Vacuolar sorting receptor (VSR) proteins bind soluble protein ligands in a sequence-specific manner and target them to the lytic vacuole in plant cells. A VSR from Arabidopsis thaliana, AtBP80b, has been successfully purified after heterologous expression in Drosophila S2 cells. The AtBP80b protein (560 amino acids) was crystallized by the hanging-drop method with a PEG 400-based precipitant. Preliminary X-ray diffraction studies of an AtBP80b crystal showed that it belongs to the cubic space group P2(1)3 (or P4(2)32) and has unit-cell parameters a = b = c = 145.9 A. Crystals of the VSR diffract beyond 2.5 A resolution.
authors.affiliation: Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USA.
authors.forename: Sally W
authors.initials: SW
authors.lastname: Rogers
authors.forename: Buhyum
authors.initials: B
authors.lastname: Youn
authors.forename: John C
authors.initials: JC
authors.lastname: Rogers
authors.forename: Chulhee
authors.initials: C
authors.lastname: Kang
mesh_terms: D000818:Animals; D017360:Arabidopsis / Q000737:chemistry*; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D001665:Binding Sites; D002460:Cell Line; D003460:Crystallization; D018360:Crystallography, X-Ray; D004330:Drosophila / Q000235:genetics; D008024:Ligands; D017434:Protein Structure, Tertiary; D033921:Vesicular Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D029681:Arabidopsis Proteins; C500310:BP80b protein, Arabidopsis; D008024:Ligands; D033921:Vesicular Transport Proteins