Crystallization and heavy-atom derivatization of StHsp14.0, a small heat-shock protein from Sulfolobus tokodaii

被引:1
|
作者
Hayashi, Takuro [1 ]
Abe, Tetsuya [2 ]
Takeda, Kazuki [1 ]
Akiyama, Nobuhiko [1 ]
Yohda, Masafumi [2 ]
Miki, Kunio [1 ,3 ]
机构
[1] Kyoto Univ, Grad Sch Sci, Dept Chem, Sakyo Ku, Kyoto 6068502, Japan
[2] Tokyo Univ Agr & Technol, Dept Biotechnol & Life Sci, Koganei, Tokyo 1848588, Japan
[3] Harima Inst, RIKEN SPring Ctr 8, Sayo, Hyogo 6795148, Japan
关键词
OLIGOMER;
D O I
10.1107/S1744309109032540
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Small heat-shock proteins (sHsps) bind and stabilize proteins denatured by heat or other stresses in order to prevent unfavourable protein aggregation. StHsp14.0 is an sHsp found in the acidothermophilic archaeon Sulfolobus tokodaii. A variant of StHsp14.0 was crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted X-rays to 1.85 angstrom resolution and belonged to space group P2(1)2(1)2, with unit-cell parameters a = 40.4, b = 61.1, c = 96.1 angstrom. The V-M value was estimated to be 2.1 angstrom(3) Da(-1), assuming the presence of two molecules in the asymmetric unit. Heavy-atom derivative crystals were prepared successfully by the cocrystallization method and are isomorphic to native crystals.
引用
收藏
页码:1007 / 1010
页数:4
相关论文
共 48 条