Cloning, overexpression, purification and crystallisation of ribosomal protein L9 from Bacillus stearothermophilus.
The cloning, sequencing and overexpression of the gene coding for Bacillus stearothermophilus ribosomal protein L9 is described. The sequence corresponds directly to that presented for the protein itself by classical methods, differing at only a few amino acid positions. The purification and crystallisation of the corresponding L9 protein is presented. The crystals are isomorphous to those described for L9 obtained by conventional methods.
Vorgias
C E
CE
European Molecular Biology Laboratory (EMBL), c/o DESY, Hamburg, Germany.
Kingswell
A J
AJ
Dauter
Z
Z
Wilson
K S
KS
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003460:Crystallization; D004269:DNA, Bacterial; D004591:Electrophoresis, Polyacrylamide Gel; D005798:Genes, Bacterial; D001411:Geobacillus stearothermophilus / Q000235:genetics*; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D012269:Ribosomal Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D014169:Transformation, Bacterial; D014961:X-Ray Diffraction
D004269:DNA, Bacterial; D012269:Ribosomal Proteins; C049650:ribosomal protein L9