EC Number |
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3.1.26.12 | apoprotein, X-ray diffraction structure determination and analysis at 3.3 resolution, modelling using molecular replacement |
3.1.26.12 | crystal structure of RNase E in complex with the sRNA RprA reveals a duplex recognition site that saddles an inter-protomer surface to help present substrates for cleavage |
3.1.26.12 | enolase bound to its cognate site from RNase E, residues 823-850, X-ray diffraction structure determination and analysis at 1.9 A resolution |
3.1.26.12 | hanging drop vapor diffusion method. The crystal structure of SSO1404 is solved at 1.6 A resolution revealing the first ribonuclease with a ferredoxin-like fold |
3.1.26.12 | PNPase complexed with the recognition site from RNase E and with manganese in the presence or in the absence of modified RNA, hanging drop vapour diffusion method, using 0.2 M ammonium nitrate and 20% w/v PEG 3350 or 0.2 M diammonium hydrogen citrate and 17% PEG 3350 |
3.1.26.12 | purified recombinant detagged isolated S1 domain, residues 35-125, large crystals grow within 4 weeks in 1.65 mM protein containing solution of 20 mM phosphate, pH 6.5, 50 mM NaCl, and 0.05% w/v NaN3 at 4°C, isomorphous crystals are grown by hanging drop vapour diffusion method at 18°C, 1.3 mM protein in 20 mM HEPES, p 6.5, 50 mM NaCl, is mixed with a well solution containing 0.17 M sodium acetate, pH 6.5, 85 mM sodium cacodylate, 50% w/v PEG 8000, and 15% glycerol, X-ray diffraction structure determination and analysis at 2.0 A resolution using single anomalous dispersion or trimethyl lead(IV) acetate derivatives |
3.1.26.12 | purified recombinant His-tagged N-terminal RNaseE catalytic N domain, vapour diffusion method, 7 mg/ml protein in solution is mixed in a 1:1 ratio with precipitation solution containing 0.18 M Li2SO4, 0.09 M Tris-HCl, pH 8.5, 27% w/v PEG 4000, and 10% v/v glycerol, X-ray diffraction structure determination and analysis at 3.4 A resolution |
3.1.26.12 | RNase E catalytic domain in the apo-state, molecular replacement |
3.1.26.12 | the crystal structure of enolase bound to its cognate site from RNase E, residues 823-850, at 1.9 A resolution. The structure suggests that enolase may help to organize an adjacent conserved RNA-binding motif in RNase E |
3.1.26.12 | X-ray diffraction structure determination and analysis at 2.9 A resolution |