Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA

Heli Nummelin, Yasmin El Tahir, Pauli Ollikka, Mikael Skurnik, Adrian Goldman

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

A recombinant form of a collagen-binding fragment of Yersinia enterocolitica serotype 0:3 adhesin YadA with an N-terminal polyhistidine affinity tag has been produced in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the trigonal space group R3, with unit-cell parameters a = b = 67.05, c = 221.95 Å, and diffract to 1.55 Å resolution on a synchrotron-radiation source.

Original languageEnglish
Pages (from-to)1042-1044
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume58
Issue number6 II
DOIs
Publication statusPublished - 2002

Fingerprint

Yersinia
Yersinia enterocolitica
Synchrotrons
collagens
Escherichia
Crystallization
Synchrotron radiation
radiation sources
purification
Escherichia coli
Purification
affinity
synchrotron radiation
Collagen
Vapors
fragments
vapors
Radiation
crystallization
Crystals

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Clinical Biochemistry
  • Structural Biology
  • Condensed Matter Physics

Cite this

Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA. / Nummelin, Heli; El Tahir, Yasmin; Ollikka, Pauli; Skurnik, Mikael; Goldman, Adrian.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 58, No. 6 II, 2002, p. 1042-1044.

Research output: Contribution to journalArticle

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