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Crystallization and preliminary crystallographic analysis of ribosomal protein S8 from Thermus thermophilus
Author(s) -
Tishchenko S.V.,
Vysotskaya V.S.,
Fomenkova N.P.,
Nikonov S.V.,
Ehresmann B.,
Garber M.B.
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199702)27:2<309::aid-prot15>3.0.co;2-q
Subject(s) - crystallization , thermus thermophilus , crystallography , protein crystallization , ribosomal protein , ribosomal rna , chemistry , ribosome , biochemistry , gene , rna , escherichia coli , organic chemistry
Crystals have been obtained for recombinant ribosomal protein S8 from Thermus thermophilus produced by Escherichia coli . The protein crystals have been grown in 40 mM potassium phosphate buffer (pH 6.0) in hanging drops equilibrated against saturated ammonium sulfate (unbuffered) with 2‐methyl‐2,4‐pentandiol (v/v). The crystals belong to the space group P4 1(3) 2 1 2 with cell parameters a = b = 67.65 Å, c = 171.12 Å. They diffract x‐rays to 2.9 Å resolution. © 1997 Wiley‐Liss, Inc.