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

Kenji Murata, Andrew J Fisher, Jerry L. Hedrick

Research output: Contribution to journalArticle

6 Citations (Scopus)

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 (VM = 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.

Original languageEnglish (US)
Article numberfw5135
Pages (from-to)396-398
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number5
DOIs
StatePublished - Apr 28 2007

Fingerprint

Salmon
eggs
X ray analysis
Crystallization
Lectins
Ovum
X-Rays
crystallization
Crystals
Affinity chromatography
Synchrotrons
x rays
crystals
Synchrotron radiation
Affinity Chromatography
fertilization
Fertilization
Eggs
chromatography
Vapors

Keywords

  • Lectins
  • Polyspermy
  • Salmon

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

Crystallization and X-ray analysis of the salmon-egg lectin SEL24K. / Murata, Kenji; Fisher, Andrew J; Hedrick, Jerry L.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 63, No. 5, fw5135, 28.04.2007, p. 396-398.

Research output: Contribution to journalArticle

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