Cloning, expression, and crystallization of Cpn60 proteins from Thermococcus litoralis.

J Osipiuk; M Sriram; X Mai; M W Adams; A Joachimiak

doi:10.18388/abp.2000_4079

Cloning, expression, and crystallization of Cpn60 proteins from Thermococcus litoralis.

J Osipiuk Argonne National Laboratory, Biosciences Division, IL 60439, USA.;
M Sriram
X Mai
M W Adams
A Joachimiak

DOI: https://doi.org/10.18388/abp.2000_4079

Abstract

Two genes of the extreme thermophilic archaeon Thermococcus litoralis homologous to those that code for Cpn60 chaperonins were cloned and expressed in Escherichia coli. Each of the Cpn60 subunits as well as the entire Cpn60 complex crystallize in a variety of morphological forms. The best crystals diffract to 3.6 A resolution at room temperature and belong to the space group 1422 with unit cell parameters a = b = 193.5 A, c = 204.2 A.

Published

2000-03-31

Issue

Vol. 47 No. 1 (2000)

Section

Articles

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