Crystals of a mutant form of ribosomal protein L22 rendering bacterial ribosomes resistant to erythromycin.
A mutant form of Thermus thermophilus ribosomal protein L22 responsible for erythromycin resistance has been overexpressed in Escherichia coli, purified to homogeneity and crystallized using the hanging-drop vapour-diffusion technique. While several different crystallization conditions were found, only one set of conditions yielded crystals suitable for X-ray diffraction analysis. These crystals grow as thick plates, with unit-cell parameters a = 31.8, b = 86.59, c = 38.96 A, beta = 104.47 degrees. The crystals belong to the space group P2(1) and diffract to 1.8 A resolution. On the basis of density calculations, two monomers are predicted per asymmetric unit (V(M) = 2.06 A(3) Da(-1)), with a solvent content of 40%.
Davydova
N
N
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia. n.davydova@ic.ac.uk
Fedorov
R
R
Streltsov
V
V
Liljas
A
A
Garber
M
M
D001426:Bacterial Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004352:Drug Resistance, Microbial / Q000235:genetics; D004917:Erythromycin / Q000494:pharmacology; D029968:Escherichia coli Proteins; D009154:Mutation; D011487:Protein Conformation; D012338:RNA, Ribosomal, 23S / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D012269:Ribosomal Proteins; D016963:Thermus thermophilus / Q000737:chemistry* / Q000187:drug effects
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D012338:RNA, Ribosomal, 23S; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; C489371:rplV protein, E coli; D004917:Erythromycin