Three‐dimensional structure of lectin from pea (Pisum sativum) at 5 Å resolution

FEBS Letters

Riskulov, R.R.¹  Dobrokhotova, Z.D.¹  Myshko, G.E.¹  Lubnin, M.Yu.¹  Saprykina, L.F.¹  Mokulskaya, T.D.¹  Proskudina, L.T.¹  Rogacheva, M.M.¹  Kuzev, S.V.¹  Lobsanov, Yu.D.¹  Khrenov, A.A.¹  Mokulskii, M.A.¹ 

[1] Institute of Molecular Genetics, USSR Academy of Sciences, Kurchatov Square 46, 123182 Moscow, USSR

关键词: Lectin;    Crystal;    X-ray diffraction;    Three-dimensional structure;    Multichannel diffractometer;   

DOI  :  10.1016/0014-5793(84)80022-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The protein lectin from pea (M _r 49 000) crystallizes in space group P2₁2₁2₁ with cell dimensions a = 51.0 Å, b = 61.7 Å, c = 137.6 Å and z = 4. The three-dimensional structure of pea lectin at 5 Å 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 Å. 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.

【 授权许可】

Unknown