Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Crystallization (Commentary)

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 10
EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.12apoprotein, X-ray diffraction structure determination and analysis at 3.3 resolution, modelling using molecular replacement
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.12crystal 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.12enolase bound to its cognate site from RNase E, residues 823-850, X-ray diffraction structure determination and analysis at 1.9 A resolution
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.12hanging 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.12PNPase 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.12purified 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.12purified 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.12RNase E catalytic domain in the apo-state, molecular replacement
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.12the 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.12X-ray diffraction structure determination and analysis at 2.9 A resolution
Results 1 - 10 of 10