RIBOSOMAL-PROTEIN L22 FROM THERMUS-THERMOPHILUS - SEQUENCING, OVEREXPRESSION AND CRYSTALLIZATION

被引：8

作者：

DAVYDOVA, NL

GRYAZNOVA, OI

MASHCHENKO, OV

VYSOTSKAYA, VS

JONSSON, BH

AL-KARADAGHI, S

LILJAS, A

GARBER, MB

机构：

[1] RUSSIAN ACAD SCI, INST PROT RES, DEPT STRUCT & FUNCT RIBOSOME, PUSHCHINO 142292, RUSSIA

[2] UMEA UNIV, DEPT BIOCHEM, S-90187 UMEA, SWEDEN

来源：

FEBS LETTERS | 1995年 / 369卷 / 2-3期

关键词：

RIBOSOMAL PROTEIN; OVEREXPRESSION; PURIFICATION; CRYSTALLIZATION; THERMUS THERMOPHILUS;

D O I：

10.1016/0014-5793(95)00755-X

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：

The gene for the ribosomal protein L22 from Thermus thermophilus has been sequenced and overexpressed in Escherichia coli. A multiple sequence alignment was carried out for all proteins of the L22 family reported so far. The recombinant protein was purified and crystallized. The crystals belong to the space group P2(1)2(1)2(1), with cell parameters of a = 32.6 Angstrom, b = 66.0 Angstrom, c = 67.8 Angstrom.

引用

页码：229 / 232

页数：4

共 39 条

[21] THE NUCLEOTIDE-SEQUENCE OF THE GENES-CODING FOR THE S19 AND L22 EQUIVALENT RIBOSOMAL-PROTEINS FROM HALOBACTERIUM-HALOBIUM [J].