Structure of azurin from Alcaligenes denitrificans refinement at 1·8 Å resolution and comparison of the two crystallographically independent molecules

Journal of Molecular Biology

Volumn 203, Issue 4, 1988, Pages 1071-1095

  Baker, Edward N ^a  

^a MASSEY UNIVERSITY   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

AZURIN; BACTERIAL PROTEIN; COPPER; CYSTEINE; HISTIDINE; SULFATE;

ALCALIGENES; ARTICLE; CHEMICAL STRUCTURE; CRYSTALLIZATION; HYDROGEN BOND; PROTEIN CONFORMATION; X RAY DIFFRACTION;

ALCALIGENES; AZURIN; BACTERIAL PROTEINS; COPPER; CRYSTALLIZATION; CYSTEINE; HISTIDINE; HYDROGEN BONDING; MODELS, MOLECULAR; PROTEIN CONFORMATION; SULFATES; X-RAY DIFFRACTION;

EID: 0024293340     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/0022-2836(88)90129-5     Document Type: Article

References (62)

1. Structural Features of Azurin at 2.7 Å Resolution
2. Crystallographic refinement of the structure of actinidin at 1.7 Å resolution by fast Fourier least-squares methods
3. On the evaluation of root-mean-square errors in atomic coordinates in protein crystallography
4. Affinity Labeling of an Electron Transfer Pathway in Azurin by Cr(II) Ions
5. copper proteins systems containing the “Blue” copper center
6. A limited-range step-scan method for collecting X-ray diffraction data
7. A graphics model building and refinement system for macromolecules
8. Kinetics of long-distance ruthenium-to-copper electron transfer in [pentaammineruthenium histidine-83]azurin
9. Traitement statistique des erreurs dans la determination des structures cristallines
10. Analysis of the kinetics of electron transfer between blue copper proteins and inorganic redox agents. Reactions involving bis(dipicolinate) complexes of cobalt(III) and iron(II) and stellacyanin, plastocyanin, and azurin
11. A semi-empirical method of absorption correction
12. Spectroscopic studies on plastocyanin single crystals: a detailed electronic structure determination of the blue copper active site
13. An efficient general-purpose least-squares refinement program for macromolecular structures