Crystallization and preliminary X-ray analysis of an intact soluble-form variant surface glycoprotein from the African trypanosome, Trypanosoma brucei

  • Down J
  • Garman S
  • Gurnett A
 et al. 
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Abstract

The intact variant surface glycoprotein (VSG) ILTat 1.24 from Trypanosoma brucei has been crystallized. An amino-terminal domain of the protein comprising two thirds of the sequence had been crystallized previously after proteolytic digestion. Now intact VSG crystals have been grown from 50 mm-Mes (pH 6.5) containing 62% ( w v) saturated ammonium sulfate. The crystals are demonstrated to contain the intact VSG by h.p.l.c. gel filtration and reaction with an antibody to the inositol phosphate oligosaccharide on the VSG carboxy terminus. The space group of the crystals is P6222 (or P6422) with unit cell dimensions a = 6 = 184 A ̊ and c = 214 A ̊. Preparative isoelectric focusing may have facilitated crystallization. © 1991.

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Authors

  • James A. Down

  • Scott C. Garman

  • Anne M. Gurnett

  • Mervyn J. Turner

  • Don C. Wiley

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