Abstract
The structure of the blue copper protein azurin ( M r 14,000) from Pseudomonas aeruginosa has been determined from a 3.0 Å resolution electron density map computed with phases based on a uranyl derivative to 3 Å resolution and a platinum derivative to 3.7 Å. Interpretation of the somewhat noisy map was based on comparison of the density of the four molecules in the asymmetric unit with their averaged density. The polypeptide chain folds into an eight-strand β barrel with an additional flap containing a short helix. The copper atom is bound at one end and on the inside of the barrel, probably to a cysteine, a methionine, and two histidine residues.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
