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Title: Crystallization and X-ray analysis of the salmon-egg lectin SEL24K

Abstract

The 24 kDa egg lectin of Chinook salmon (Oncorhynchus tshawytscha) 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 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 P2{sub 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{sub M} = 2.3 Å{sup 3} Da{sup −1}), corresponding to a solvent content of 45.5%. A self-rotation function suggests an arrangement with 222 point symmetry within the asymmetric unit.

Authors:
 [1];  [2];  [1]
  1. Department of Animal Science, University of California, Davis 95616 (United States)
  2. Department of Chemistry, University of California, Davis 95616 (United States)
Publication Date:
OSTI Identifier:
22360325
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 5; Other Information: PMCID: PMC2335001; PMID: 17565179; PUBLISHER-ID: fw5135; OAI: oai:pubmedcentral.nih.gov:2335001; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; AFFINITY; CHANNELING; CRYSTALLIZATION; CRYSTALS; DIFFUSION; MOLECULES; RESOLUTION; ROTATION; SOLVENTS; SPACE GROUPS; SYMMETRY; SYNCHROTRON RADIATION; VAPORS

Citation Formats

Murata, Kenji, Fisher, Andrew J., and Hedrick, Jerry L., E-mail: jlhedrick@ucdavis.edu. Crystallization and X-ray analysis of the salmon-egg lectin SEL24K. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107015345.
Murata, Kenji, Fisher, Andrew J., & Hedrick, Jerry L., E-mail: jlhedrick@ucdavis.edu. Crystallization and X-ray analysis of the salmon-egg lectin SEL24K. United Kingdom. doi:10.1107/S1744309107015345.
Murata, Kenji, Fisher, Andrew J., and Hedrick, Jerry L., E-mail: jlhedrick@ucdavis.edu. Tue . "Crystallization and X-ray analysis of the salmon-egg lectin SEL24K". United Kingdom. doi:10.1107/S1744309107015345.
@article{osti_22360325,
title = {Crystallization and X-ray analysis of the salmon-egg lectin SEL24K},
author = {Murata, Kenji and Fisher, Andrew J. and Hedrick, Jerry L., E-mail: jlhedrick@ucdavis.edu},
abstractNote = {The 24 kDa egg lectin of Chinook salmon (Oncorhynchus tshawytscha) 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 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 P2{sub 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{sub M} = 2.3 Å{sup 3} Da{sup −1}), corresponding to a solvent content of 45.5%. A self-rotation function suggests an arrangement with 222 point symmetry within the asymmetric unit.},
doi = {10.1107/S1744309107015345},
journal = {Acta Crystallographica. Section F},
number = Pt 5,
volume = 63,
place = {United Kingdom},
year = {Tue May 01 00:00:00 EDT 2007},
month = {Tue May 01 00:00:00 EDT 2007}
}
  • No abstract prepared.
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  • The crystallization and preliminary X-ray diffraction analysis of a red marine alga lectin isolated from H. musciformis is reported. HML, a lectin from the red marine alga Hypnea musciformis, defines a novel lectin family. Orthorhombic crystals of HML belonging to space group P2{sub 1}2{sub 1}2{sub 1} grew within three weeks at 293 K using the hanging-drop vapour-diffusion method. A complete data set was collected at 2.4 Å resolution. HML is the first marine alga lectin to be crystallized.
  • The lectin from the Nigerian legume B. mildbraedii was crystallized in complex with Man(α1-2)Man and data were collected to a resolution of 1.90 Å using synchrotron radiation. The lectin from Bowringia mildbraedii seeds crystallizes in the presence of the disaccharide Man(α1-2)Man. The best crystals grow at 293 K within four weeks after a pre-incubation at 277 K to induce nucleation. A complete data set was collected to a resolution of 1.90 Å using synchrotron radiation. The crystals belong to space group I222, with unit-cell parameters a = 66.06, b = 86.35, c = 91.76 Å, and contain one lectin monomermore » in the asymmetric unit.« less