Crystal structure of the F7A mutant of the cytochrome c551 from Pseudomonas aeruginosa
Unveiling a Hidden Folding Intermediate in c-Type Cytochromes by Protein Engineering
Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 A resolution and comparison of the two redox forms.
Selected mutations in a mesophilic cytochrome c confer the stability of a thermophilic counterpart.
An obligatory intermediate in the folding pathway of cytochrome c552 from Hydrogenobacter thermophilus.
EDPEVLAKNKGCVACHAIDTKMVGPAYKDVAAKFAGQAGAEAELAQRIKNGSQGVWGPIPMPPNAVSDDEAQTLAKWVLS QK
26-30% PEG 4K, zinc acetate 0.2 M, sodium acetate 0.1 M, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K
Crystal structure of cyt c551 from Pseudomonas aeruginosa
Quintuple mutant of cyt c551 from Pseudomonas aeruginosa
Hydrogenobacter thermophilus cyt c552, a thermophilic homologue of Pseudomonas aeruginosa cyt c551
HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
cytochrome c, alpha helix, heme c, ELECTRON TRANSPORT
EDPEVLFKNKGCVACHAIDTKMVGPAYKDVAAKFAGQAGAEAELAQRIKNGSQGVWGPIPMPPNAVSDDEAQTLAKWVLS QK