title: Crystallization and preliminary X-ray crystallographic studies of the ice-binding protein from the Arctic [correction of Aantarctic] yeast Leucosporidium sp. AY30.
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(3)2(1)2, 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.
authors.affiliation: Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, Republic of Korea.
authors.forename: Ae Kyung
authors.initials: AK
authors.lastname: Park
authors.forename: Kyoung Sun
authors.initials: KS
authors.lastname: Park
authors.forename: Hak Jun
authors.initials: HJ
authors.lastname: Kim
authors.forename: Hyun
authors.initials: H
authors.lastname: Park
authors.forename: In Young
authors.initials: IY
authors.lastname: Ahn
authors.forename: Young Min
authors.initials: YM
authors.lastname: Chi
authors.forename: Jin Ho
authors.initials: JH
authors.lastname: Moon
mesh_terms: D001487:Basidiomycota / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry*
chemical_list: D005656:Fungal Proteins