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Crystallization and preliminary X-ray diffraction analysis of the lectin from Dioclea rostrata Benth seeds
- Publication Year :
- 2006
- Publisher :
- International Union of Crystallography, 2006.
-
Abstract
- Lectins from the Diocleinae subtribe (Leguminosae) are highly similar proteins that promote various biological activities with distinctly differing potencies. The structural basis for this experimental data is not yet fully understood. Dioclea rostrata lectin was purified and crystallized by hanging-drop vapour diffusion at 293 K. The crystal belongs to the orthorhombic space group I222, with unit-cell parameters a = 61.51, b = 88.22, c = 87.76 A. Assuming the presence of one monomer per asymmetric unit, the solvent content was estimated to be about 47.9%. A complete data set was collected at 1.87 A resolution.
- Subjects :
- Biophysics
Crystallography, X-Ray
Biochemistry
law.invention
Crystal
chemistry.chemical_compound
Structural Biology
law
Genetics
Crystallization
biology
Resolution (electron density)
Space group
Lectin
Fabaceae
Condensed Matter Physics
Crystallography
Monomer
chemistry
Crystallization Communications
X-ray crystallography
Seeds
biology.protein
Orthorhombic crystal system
Plant Lectins
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....da4cbc9c88b397bc226d42b1b4525fe7