Expression of a selenomethionine derivative and preliminary crystallographic studies of human cystatin C

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Abstract

Human cystatin C, a protein with amyloidogenic properties and a potent inhibitor of papain-like mammalian proteases, has been produced in its full-length form by recombinant techniques and crystallized in two polymorphic forms: cubic and tetragonal. A selenomethionyl derivative of the protein, obtained by Escherichia coli expression and with complete Met→Se-Met substitution confirmed by mass spectrometry, amino-acid analysis and X-ray absorption spectra, was crystallized in the cubic form. A truncated variant of the protein, lacking ten N-terminal residues, has also been crystallized. The crystals of this variant are tetragonal and, like the two polymorphs of the full-length protein, contain multiple copies of the molecule in the asymmetric unit, suggesting oligomerization of the protein.

Detaljer

Författare
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Strukturbiologi

Nyckelord

Originalspråkengelska
Sidor (från-till)1939-1942
TidskriftActa Crystallographica. Section D: Biological Crystallography
Volym55
Utgåva nummer11
StatusPublished - 1999
PublikationskategoriForskning
Peer review utfördJa