PURIFICATION, CHARACTERIZATION AND CRYSTALLIZATION OF ACANTHAMOEBA PROFILIN EXPRESSED IN ESCHERICHIA-COLI

被引：32

作者：

ALMO, SC

POLLARD, TD

WAY, M

LATTMAN, EE

机构：

[1] WHITEHEAD INST BIOMED RES,CAMBRIDGE,MA 02139

[2] JOHNS HOPKINS UNIV,SCH MED,DEPT CELL BIOL & ANAT,BALTIMORE,MD 21205

[3] JOHNS HOPKINS UNIV,SCH MED,DEPT BIOPHYS,BALTIMORE,MD 21205

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1994年 / 236卷 / 03期

关键词：

PROFILIN; CYTOSKELETON; CRYSTALLIZATION; EXPRESSION; PROTEIN STRUCTURE;

D O I：

10.1006/jmbi.1994.1200

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：

Profilin (isoform I) from Acanthamoeba castellani was expressed in Escherichia coli using a bacteriophage T7-based expression vector. The recombinant material is similar to authentic profilm from Acanthamoeba-based on fluorescence monitored urea denaturation, circular dichroisrn, actin-nuoleotide exchange rate and the Ka for rabbit skeletal actin. This recombinant material crystallized from 80% saturated sodium potassium tartrate, yielding monoclinic crystals, space group C2, a = 91·4 Å, b =37·4 Å, c = 34·7 Å, α =109·6°. These crystals contain one molecule in the asymmetric unit and diffract to 2·0 Å. © 1994 Academic Press, Inc.

引用

页码：950 / 952

页数：3

共 20 条

[1] SPECTROPHOTOMETRIC STUDY OF THE REACTION OF PROTEIN SULFHYDRYL GROUPS WITH ORGANIC MERCURIALS [J].