Ribosomal protein L22 from Thermus thermophilus: sequencing, overexpression and crystallisation.
The gene for the ribosomal protein L22 from Thermus thermophilus has been sequenced and overexpressed in Escherichia coli. A multiple sequence alignment was carried out for all proteins of the L22 family reported so far. The recombinant protein was purified and crystallized. The crystals belong to the space group P2(1)2(1)2(1), with cell parameters of a = 32.6 A, b = 66.0 A, c = 67.8 A.
Davydova
N L
NL
Molecular Biophysics, University of Lund, Sweden.
Gryaznova
O I
OI
Mashchenko
O V
OV
Vysotskaya
V S
VS
Jonsson
B H
BH
al-Karadaghi
S
S
Liljas
A
A
Garber
M B
MB
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial / Q000235:genetics*; D008969:Molecular Sequence Data; D016601:RNA-Binding Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification; D012269:Ribosomal Proteins; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D016963:Thermus thermophilus / Q000235:genetics*
D029968:Escherichia coli Proteins; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; D012269:Ribosomal Proteins; C489371:rplV protein, E coli