MEASUREMENT OF THE RADII OF GYRATION OF RIBOSOMAL COMPONENTS INSITU BY NEUTRON-SCATTERING

被引：9

作者：

HARRISON, DH

MAY, RP

MOORE, PB

机构：

[1] YALE UNIV, DEPT MOLEC BIOPHYS & BIOCHEM, NEW HAVEN, CT 06520 USA

[2] INST MAX VON LAUE PAUL LANGEVIN, F-38042 GRENOBLE, FRANCE

来源：

JOURNAL OF APPLIED CRYSTALLOGRAPHY | 1993年 / 26卷 / pt 2期

关键词：

D O I：

10.1107/S0021889892010069

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The radii of gyration of 16S rRNA, 30S proteins and S4 have been measured in situ in the 30S ribosomal subunit from Escherichia coli by the three-isotope method (TIM) [Pavlov & Serdyuk (1987). J. Appl. Cryst. 20, 105-110]. The values obtained were 70.0 (25), 66.7 (24) and 23.5 (10) angstrom, respectively. The data for ribosomal protein and RNA in this system are consistent with earlier findings, verifying that the TIM is reliable. The estimate obtained for S4 is one of the first high-quality estimates of the radius of gyration obtained for a ribosomal protein in situ.

引用

页码：198 / 206

页数：9

共 23 条

[1]

CAPEL MS, 1988, METHOD ENZYMOL, V164, P532

[2] POSITIONS OF S2, S13, S16, S17, S19 AND S21 IN THE 30-S-RIBOSOMAL SUBUNIT OF ESCHERICHIA-COLI [J].