Journal article
Purification, crystallization and preliminary crystallographic studies of the ligand-binding domain of a plant vacuolar sorting receptor
Acta crystallographica. Section D, Biological crystallography., Vol.60(Pt 11), pp.2028-2030
11/2004
Handle:
https://hdl.handle.net/2376/116442
PMID: 15502317
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.
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Details
- Title
- Purification, crystallization and preliminary crystallographic studies of the ligand-binding domain of a plant vacuolar sorting receptor
- Creators
- Sally W Rogers - Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USABuhyum YounJohn C RogersChulhee Kang
- Publication Details
- Acta crystallographica. Section D, Biological crystallography., Vol.60(Pt 11), pp.2028-2030
- Academic Unit
- Chemistry, Department of
- Publisher
- United States
- Identifiers
- 99900548082301842
- Language
- English
- Resource Type
- Journal article