1. Three-dimensional structure of lectin from pea (Pisum sativum) at 5 Å resolution
- Author
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R.R. Riskulov, T. D. Mokulskaya, M. A. Mokulskii, A. A. Khrenov, M.Yu. Lubnin, Yu.D. Lobsanov, G. E. Myshko, L.F. Saprykina, S. V. Kuzev, L.T. Proskudina, M.M. Rogacheva, and Z. D. Dobrokhotova
- Subjects
biology ,Multiple isomorphous replacement ,Dimer ,Resolution (electron density) ,Biophysics ,Lectin ,Cell Biology ,Crystal structure ,biology.organism_classification ,Three-dimensional structure ,Biochemistry ,X-ray diffraction ,Pisum ,Crystallography ,chemistry.chemical_compound ,chemistry ,Structural Biology ,Concanavalin A ,Crystal ,Multichannel diffractometer ,Genetics ,biology.protein ,Molecule ,Molecular Biology - Abstract
The protein lectin from pea ( M r 49 000) crystallizes in space group P2 1 2 1 2 1 with cell dimensions a = 51.0 A, b = 61.7 A, c = 137.6 A and z = 4. The three-dimensional structure of pea lectin at 5 A resolution was determined by multiple isomorphous replacement method. The data were collected on an ARGUS multichannel diffractometer. The pea lectin molecule can be described as a dimer with approximate dimensions 85 × 55 × 40 A. The borderline between the globules appears in the three-dimensional model as a shallow groove on its surface. Both globules have two dense layers. The molecule proved to be quite similar to the dimer of concanavalin A.
- Published
- 1984
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