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Crystallization and preliminary crystallographic analysis of ribosomal protein S8 from Thermus thermophilus

✍ Scribed by S.V. Tishchenko; V.S. Vysotskaya; N.P. Fomenkova; S.V. Nikonov; B. Ehresmann; M.B. Garber

Publisher: John Wiley and Sons
Year: 1997
Tongue: English
Weight: 65 KB
Volume: 27
Category: Article
ISSN: 0887-3585
DOI: 10.1002/(sici)1097-0134(199702)27:2<309::aid-prot15>3.0.co;2-q

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✦ Synopsis

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 5 b 5 67.65 Å, c 5 171.12 Å. They diffract x-rays to 2.9 Å resolution. Proteins

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