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EC Number
Crystallization
Reference
1.2 A resolution
crystal structure of HpMCAT at 2.5 A resolution is shown. HpMCAT has a compact folding composed of a large subdomain with a similar core as in alpha/beta hydrolases, and a similar ferredoxin-like small subdomain as in acylphosphatases
crystal structure of MCAT is determined to 2.3 A
crystal structure of Mycobacterium tuberculosis MCAT (mtFabD) is determined to 3.0 A resolution by multi-wavelength anomalous dispersion. Phasing is facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD
crystal structures of MCAT from Staphylococcus aureus and Streptococcus pneumoniae are determined at 1.46 and 2.1 A resolution, respectively
crystal structures of MCAT from Staphylococcus aureus and Streptococcus pneumoniae are determined at 1.46 and 2.1 A resolution, respectively. In the SaMCAT structure, the N-terminal expression peptide of a neighboring molecule running in the opposite direction of malonyl-CoA makes extensive interactions with the highly conserved Gly-Gln-Gly-Ser-Gln stretch, suggesting a new design platform
mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase by protein crystallography
purified recombinant enzyme, X-ray diffraction structure determination and analysis
recombinant purified enzyme, 3 mg/ml protein in 10 mM Tris-HCl, pH 7.4, 1 mM 2-mercaptoethanol, hanging drop vapoir diffusion method, 3 days, room temperature, soaking of crystals in 30% PEG 4000, 100 mM sodium acetate, pH 4.8, 200 mM ammonium acetate, and 20% glycerol for cryoprotection, X-ray diffraction structure determination and analysis at 2.0 A resolution, macromolecular docking simulation with K47A/K190A/R287A/K293A mutant actinorhodin ACP structure, overview
the crystal structure of malonyl CoA-acyl carrier protein transacylase (XoMCAT) is determined at 2.3 A resolution in complex with N-cyclohexyl-2-aminoethansulfonic acid
Results 1 - 10 of 11 > >>