Literature DB >> 897666

Cholera toxin crystals suitable for x-ray diffraction.

P B Sigler, M E Dryan, H C Kiuefer, R A Finkelstein.   

Abstract

Large crystals of the cholera toxin were grown; their dimensions, symmetry (P21), order, and resistance to radiation make them ideally suited for a high-resolution x-ray structure determination. There is one molecule (approximately 84,000 daltons) per asymmetric unit, and therefore the lattice reveals no molecular symmetry. Two distinct bioassays indicate that the protein from dissolved crystals retains full biological activity.

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Year:  1977        PMID： 897666     DOI： 10.1126/science.197.4310.1277-a

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  5 in total

1.  Two-dimensional crystals of cholera toxin B-subunit-receptor complexes: projected structure at 17-A resolution.

Authors:  D S Ludwig; H O Ribi; G K Schoolnik; R D Kornberg
Journal:  Proc Natl Acad Sci U S A       Date:  1986-11       Impact factor: 11.205

2.  Quantitative description of the binding of GM1 oligosaccharide by cholera enterotoxin.

Authors:  D E Schafer; A K Thakur
Journal:  Cell Biophys       Date:  1982-03

Review 3.  Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin.

Authors:  B D Spangler
Journal:  Microbiol Rev       Date:  1992-12

4.  Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution.

Authors:  V S Allured; R J Collier; S F Carroll; D B McKay
Journal:  Proc Natl Acad Sci U S A       Date:  1986-03       Impact factor: 12.779

5.  Subunit number and arrangement in Escherichia coli heat-labile enterotoxin.

Authors:  D M Gill; J D Clements; D C Robertson; R A Finkelstein
Journal:  Infect Immun       Date:  1981-09       Impact factor: 3.441
  5 in total

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