Three‐dimensional structure of lectin from pea (Pisum sativum) at 5 Å resolution
- 2 January 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 165 (1) , 97-100
- https://doi.org/10.1016/0014-5793(84)80022-8
Abstract
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.Keywords
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