Crystallization and preliminary X-ray crystallographic studies of the ice-binding protein from the Antarctic yeast Leucosporidium sp. AY30

Ae Kyung Park, Kyoung Sun Park, Hak Jun Kim, Hyun Park, In Young Ahn, Young Min Chi, Jin Ho Moon

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Freezing is dangerous to cellular organisms because it causes an increase in the concentration of ions and other solutes in the plasma, denatures biomolecules and ruptures cell membranes. Some cold-adapted organisms can survive at subzero temperatures by producing proteins that bind to and inhibit the growth of ice crystals. To better understand the structure and function of these proteins, the ice-binding protein from Leucosporidium sp. AY30 (LeIBP) was overexpressed, purified and crystallized. The native crystal belonged to space group P4 32 12, with unit-cell parameters a = b = 98.05, c = 106.13 Å. Since LeIBP lacks any cysteine or methionine residues, two leucine residues (Leu69 and Leu155) were substituted by methionine residues in order to obtain selenomethionine-substituted LeIBP for use in multiple-wavelength anomalous diffraction (MAD) phasing. The selenomethionine-substituted mutant crystallized in the same space group as the native protein.

Original languageEnglish
Pages (from-to)800-802
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number7
DOIs
Publication statusPublished - 2011 Jul

Keywords

  • Antarctic yeast
  • cold-adaptation
  • freezing
  • ice-binding proteins

ASJC Scopus subject areas

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

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