Crystallization of isoelectrically homogeneous cholera toxin
- Argonne National Laboratory, IL (USA)
Past difficulty in growing good crystals of cholera toxin has prevented the study of the crystal structure of this important protein. The authors have determined that failure of cholera toxin to crystallize well has been due to its heterogeneity. They have now succeeded in overcoming the problem by isolating a single isoelectric variant of this oligomeric protein (one A subunit and five B subunits). Cholera toxin purified by their procedure readily forms large single crystals. The crystal form has been described previously. They have recorded data from native crystals of cholera toxin to 3.0-{angstrom} resolution with our electronic area detectors. With these data, they have found the orientation of a 5-fold symmetry axis within these crystals, perpendicular to the screw dyad of the crystal. They are now determining the crystal structure of cholera toxin by a combination of multiple heavy-atom isomorphous replacement and density modification techniques, making use of rotational 5-fold averaging of the B subunits.
- DOE Contract Number:
- W-31-109-ENG-38
- OSTI ID:
- 5562125
- Journal Information:
- Biochemistry; (USA), Vol. 28:3; ISSN 0006-2960
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
TOXINS
CRYSTALLIZATION
CHOLERA
ELECTROPHORESIS
ION EXCHANGE CHROMATOGRAPHY
X-RAY DIFFRACTION
ANTIGENS
BACTERIAL DISEASES
CHROMATOGRAPHY
COHERENT SCATTERING
DIFFRACTION
DISEASES
INFECTIOUS DISEASES
MATERIALS
PHASE TRANSFORMATIONS
SCATTERING
SEPARATION PROCESSES
TOXIC MATERIALS
550602* - Medicine- External Radiation in Diagnostics- (1980-)
550201 - Biochemistry- Tracer Techniques