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

J. Osipiuk | Zendy; M Sriram | Zendy; X. Mai | Zendy; Michael W. W. Adams | Zendy; A. Joachimiak | Zendy

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

Author(s) -

J. Osipiuk,

M Sriram,

X. Mai,

Michael W. W. Adams,

A. Joachimiak

Publication year - 2000

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2000_4079

Subject(s) - chaperonin , thermophile , cloning (programming) , escherichia coli , thermococcus , gene , archaea , biology , computational biology , genetics , bacteria , computer science , programming language

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.

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