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

Authors
Park, Ae KyungPark, Kyoung SunKim, Hak JunPark, HyunAhn, In YoungChi, Young MinMoon, Jin Ho
Issue Date
7월-2011
Publisher
INT UNION CRYSTALLOGRAPHY
Keywords
Antarctic yeast; cold-adaptation; freezing; ice-binding proteins
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.67, pp.800 - 802
Indexed
SCOPUS
Journal Title
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume
67
Start Page
800
End Page
802
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/112045
DOI
10.1107/S1744309111018446
ISSN
2053-230X
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 angstrom. Since LeIBP lacks any cysteine or methionine residues, two leucine residues (Leu69 and Leu155) were substituted by methionine residues in order to obtain selenomethioninesubstituted LeIBP for use in multiple-wavelength anomalous diffraction (MAD) phasing. The selenomethionine-substituted mutant crystallized in the same space group as the native protein.
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