Structure of a unique twofold symmetric haem-binding site

[1]  B. Gallois,et al.  A crystallographic study of haem binding to ferritin. , 1994, Acta crystallographica. Section D, Biological crystallography.

[2]  H. Eklund,et al.  Substitution of manganese for iron in ribonucleotide reductase from Escherichia coli. Spectroscopic and crystallographic characterization. , 1994, The Journal of biological chemistry.

[3]  J. Yariv,et al.  Location of haem in bacterioferritin of E. coli. , 1993, Acta Crystallographica Section D: Biological Crystallography.

[4]  Liang Tong,et al.  REPLACE, a suite of computer programs for molecular-replacement calculations , 1993 .

[5]  R. Prince,et al.  Direct observation of bis-sulfur ligation to the heme of bacterioferritin , 1993 .

[6]  P. Harrison,et al.  Haem and non-haem iron sites in Escherichia coli bacterioferritin: spectroscopic and model building studies. , 1993, The Biochemical journal.

[7]  J. Briat Iron assimilation and storage in prokaryotes. , 1992, Journal of general microbiology.

[8]  C. Slaughter,et al.  Unification of the ferritin family of proteins. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[9]  J. Briat,et al.  Purification, characterization and function of bacterioferritin from the cyanobacterium Synechocystis P.C.C. 6803. , 1992, The Biochemical journal.

[10]  M. Katharine Holloway,et al.  X-Ray Crystal Structure of the HIV Protease Complex with L-700,417, an Inhibitor with Pseudo C2 Symmetry , 1991 .

[11]  P. Kraulis A program to produce both detailed and schematic plots of protein structures , 1991 .

[12]  G. Moore,et al.  Bis-methionine axial ligation of haem in bacterioferritin from Pseudomonas aeruginosa , 1990, Nature.

[13]  D. Norbeck,et al.  Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor complexed to HIV-1 protease. , 1990, Science.

[14]  Hans Eklund,et al.  Three-dimensional structure of the free radical protein of ribonucleotide reductase , 1990, Nature.

[15]  P. Harrison,et al.  Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of Escherichia coli K-12 , 1989, Journal of bacteriology.

[16]  P. Harrison,et al.  Amino acid sequence of the bacterioferritin (gytochrome b1) of Escherichia coli-K12 , 1989 .

[17]  P. Harrison,et al.  Molecular size and symmetry of the bacterioferritin of Escherichia coli. X-ray crystallographic characterization of four crystal forms. , 1989, Journal of molecular biology.

[18]  R. Dickerson,et al.  Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8 A and comparison with the ferrocytochrome structure. , 1981, Journal of molecular biology.

[19]  R. Dickerson,et al.  Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution. , 1981, Journal of molecular biology.

[20]  T. A. Jones,et al.  A graphics model building and refinement system for macromolecules , 1978 .

[21]  D. Stammers,et al.  Electron density map of apoferritin at 2.8-Å resolution , 1978, Nature.

[22]  W. A. Bulen,et al.  A hemoprotein from azotobacter containing non-heme iron: isolation and crystallization. , 1973, Biochemical and biophysical research communications.

[23]  S. Deeb,et al.  CRYSTALLINE CYTOCHROME B1 FROM ESCHERICHIA COLI. , 1964, The Journal of biological chemistry.

[24]  D. Keilin Cytochrome and the Supposed Direct Spectfoscopic Observation of Oxidase , 1934, Nature.