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Crystallization and X‐ray analysis of the salmon‐egg lectin SEL24K
Author(s) -
Murata Kenji,
Fisher Andrew J.,
Hedrick Jerry L.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107015345
Subject(s) - crystallization , lectin , chemistry , crystallography , materials science , biophysics , biology , biochemistry , organic chemistry
The 24 kDa egg lectin of Chinook salmon ( Oncorhynchus tshawytscha ) is released from the egg during the cortical reaction. The lectin functions in blocking polyspermy during the fertilization process. The egg lectin was purified by affinity chromatography from salmon eggs and crystallized by the hanging‐drop vapor‐diffusion method using 15/4 EO/OH (pentaerythritol ethoxylate) as a precipitant. The crystal diffracted synchrotron‐radiation X‐rays to 1.63 Å resolution. The crystal belongs to the monoclinic space group P 2 1 , with unit‐cell parameters a = 93.0, b = 73.6, c = 113.6 Å, α = 90, β = 92.82, γ = 90°. The crystal is likely to contain eight molecules in the asymmetric unit ( V M = 2.3 Å 3  Da −1 ), corresponding to a solvent content of 45.5%. A self‐rotation function suggests an arrangement with 222 point symmetry within the asymmetric unit.

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