Three-dimensional structure of lectin from pea (Pisum sativum) at 5 Å resolution
| Autor: | 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, Z. D. Dobrokhotova |
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| Rok vydání: | 1984 |
| Předmět: |
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 |
| Zdroj: | FEBS Letters. 165:97-100 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(84)80022-8 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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