title: Cloning, expression, and crystallization of Cpn60 proteins from Thermococcus litoralis.
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.
authors.affiliation: Argonne National Laboratory, Biosciences Division, IL 60439, USA.
authors.forename: J
authors.initials: J
authors.lastname: Osipiuk
authors.forename: M
authors.initials: M
authors.lastname: Sriram
authors.forename: X
authors.initials: X
authors.lastname: Mai
authors.forename: M W
authors.initials: MW
authors.lastname: Adams
authors.forename: A
authors.initials: A
authors.lastname: Joachimiak
mesh_terms: D018833:Chaperonins / Q000737:chemistry / Q000235:genetics*; D003001:Cloning, Molecular; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D011487:Protein Conformation; D019712:Thermococcus / Q000235:genetics* / Q000378:metabolism
chemical_list: D018833:Chaperonins