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Crystallization and preliminary X‐ray crystallographic analysis of Ca 2+ ‐independent and Ca 2+ ‐dependent species of the type II antifreeze protein
Author(s) -
Nishimiya Yoshiyuki,
Kondo Hidemasa,
Yasui Masanori,
Sugimoto Hiroshi,
Noro Natsuko,
Sato Ryoko,
Suzuki Mamoru,
Miura Ai,
Tsuda Sakae
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106015570
Subject(s) - crystallization , crystallography , antifreeze protein , resolution (logic) , crystal structure , crystal (programming language) , x ray crystallography , diffraction , chemistry , type (biology) , physics , biology , optics , biochemistry , organic chemistry , artificial intelligence , computer science , programming language , ecology
Ca 2+ ‐independent and Ca 2+ ‐dependent species of the type II antifreeze protein (AFP) were both crystallized using the hanging‐drop vapour‐diffusion method. It appeared that the crystal of the Ca 2+ ‐independent species from Brachyosis rostratus belongs to space group P 2 1 2 1 2 1 , with unit‐cell parameters a  = 43.3, b  = 48.4, c = 59.7 Å, and diffraction data were collected to 1.34 Å resolution. For the Ca 2+ ‐dependent type II AFP species from Hypomesus nipponensis , crystallization was carried out for its Ca 2+ ‐free and Ca 2+ ‐bound states. 1.25 Å resolution data were collected from the crystal in the Ca 2+ ‐free state, which exhibited P 3 1 21 (or P 3 2 21) symmetry, with unit‐cell parameters a  =  b  = 66.0, c  = 50.3 Å. Data collection could be extended to 1.06 Å resolution for the crystal in the Ca 2+ ‐bound state, which appeared to be isomorphous to the crystal in the Ca 2+ ‐free state (unit‐cell parameters a = b = 66.0, c = 49.8 Å). These data will allow us to determine the high‐resolution structures of the two species of type II AFP.

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