Purification, crystallization and preliminary crystallographic study of neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2

Garry Taylor, Eric Vimr, Elspeth Garman, Graeme Laver

Research output: Contribution to journalArticlepeer-review

Abstract

The nanH genes of Vibrio cholerae and Salmonella typhimurium LT2 coding neuraminidase were cloned separately in Escherichia coli, and the expression products purified. Single crystals of the V. cholerae neuraminidase were obtained using the hanging drop vapour diffusion method with polyethylene glycol as precipitant at pH 7·2. The crystals belong to the orthorhombic space group P212121, with unit cell dimensions a = 71·9 A ̊, b = 79·0 A ̊, c = 165·7 A ̊, and with one molecule in the asymmetric unit. Diffraction extends to at least 2·5 Å. Single crystals of the S. typhimurium neuraminidase were obtained by hanging drop with potassium phosphate as precipitant at pH 7·2. The crystals also belong to the orthorhombic space group P212121, with unit cell dimensions a = 47·4 A ̊, b = 82.8 A ̊, c = 92·4 A ̊, and with one molecule in the asymmetric unit. Diffraction extends to at least 1·8 Å.

Original languageEnglish (US)
Pages (from-to)1287-1290
Number of pages4
JournalJournal of Molecular Biology
Volume226
Issue number4
DOIs
StatePublished - May 20 1992

Keywords

  • Salmonella
  • cholera
  • neuraminidase
  • sialidase

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Purification, crystallization and preliminary crystallographic study of neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2'. Together they form a unique fingerprint.

Cite this