The symmetry of Escherichia coli cpn60 (GroEL) determined by X-ray crystallography

Author:

Anders Svensson L.,Surin Brian P.,Dixon Nicholas E.,Spangfort Michael D.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference19 articles.

1. X-ray diffraction studies of the structure of satellite tobacco necrosis virus;Åkervall,1972

2. The SERC (U.K.) collaborative computing project No. 4, a suite of programs for protein crystallography;CCP4,1979

3. The Fast Rotation Function;Crowther,1972

4. Molecular chaperones;Ellis;Annu. Rev. Biochem.,1991

5. MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement;Fitzgerald;J. Appl. Crystallogr.,1988

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2. Cytoskeletal Cytoplasmic Filament Ribbon of Treponema: A Member of an Intermediate-Like Filament Protein Family;Journal of Molecular Microbiology and Biotechnology;2006

3. Imaging Individual Chaperonin and Immunoglobulin G Molecules with Scanning Tunneling Microscopy;Langmuir;1996-01-01

4. Chaperones;Circular Dichroism and the Conformational Analysis of Biomolecules;1996

5. Isolation and biochemical characterization of highly purified Escherichia coli molecular chaperone Cpn60 (GroEL) by affinity chromatography and urea-induced monomerization;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1995-09

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