Crystallization and preliminary crystallographic analysis of ribosomal protein S8 from Thermus thermophilus.
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 A, c = 171.12 A. They diffract x-rays to 2.9 A resolution.
Tishchenko
S V
SV
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
Vysotskaya
V S
VS
Fomenkova
N P
NP
Nikonov
S V
SV
Ehresmann
B
B
Garber
M B
MB
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D012269:Ribosomal Proteins / Q000737:chemistry*; D016963:Thermus thermophilus / Q000737:chemistry*
D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; D012269:Ribosomal Proteins; C030254:ribosomal protein S8