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Acta Crystallogr Sect F Struct Biol Cryst Commun. May 1, 2007; 63(Pt 5): 396–398.
Published online Apr 6, 2007. doi:  10.1107/S1744309107015345
PMCID: PMC2335001
Crystallization and X-ray analysis of the salmon-egg lectin SEL24K
Kenji Murata,a Andrew J. Fisher,b and Jerry L. Hedricka*
aDepartment of Animal Science, University of California, Davis 95616, USA
bDepartment of Chemistry, University of California, Davis 95616, USA
Correspondence e-mail: jlhedrick/at/ucdavis.edu
Received March 14, 2007; Accepted March 29, 2007.
Abstract
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 P21, 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 Å3 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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