Two-dimensional crystals of reconstituted β-subunits of the chaperonin TF55 from Sulfolobus shibatae

被引：21

作者：

Koeck, PJB ^{[1
]}

Kagawa, HK

Ellis, MJ

Hebert, H

Trent, JD

机构：

[1] Karolinska Inst, Novum, Dept Biosci, S-14157 Huddinge, Sweden

[2] Argonne Natl Lab, Ctr Mechanist Biol & Biotechnol, Argonne, IL 60439 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1998年 / 1429卷 / 01期

关键词：

two-dimensional protein crystal; transmission electron microscopy; chaperonin; TF55; archaeon; (Sulfolobus shibatae);

D O I：

10.1016/S0167-4838(98)00218-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have obtained 2-dimensional crystals of the P-subunits of the chaperonin TF55 from Sulfolobus shibatae reconstituted into oligomers in the absence of alpha-subunits. The subunits form rings with 9-fold rotational symmetry which arrange themselves in a trigonal lattice. From electron micrographs of negatively stained specimens we have calculated a projection map in plane group p312 showing the rings in top-view. (C) 1998 Elsevier Science B.V. All rights reserved.

引用

页码：40 / 44

页数：5

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