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

Kozak, M; Jankowska, E; Janowski, R; Grzonka, Z; Grubb, Anders LU ; Alvarez-Fernandez, M; Abrahamson, Magnus LU and Jaskolski, M (1999) In Acta Crystallographica. Section D: Biological Crystallography 55(11). p.1939-1942
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
cysteine proteases, protease inhibitors, cystatins, selenomethionyl derivatives
in
Acta Crystallographica. Section D: Biological Crystallography
volume
55
issue
11
pages
1939 - 1942
publisher
International Union of Crystallography
external identifiers
  • scopus:0033231140
ISSN
1399-0047
DOI
10.1107/S090744499901121X
language
English
LU publication?
yes
id
9ec984a8-b6bb-469e-9ae6-dcab3a84de43 (old id 1115943)
date added to LUP
2008-07-09 13:12:34
date last changed
2017-01-01 07:02:38
@article{9ec984a8-b6bb-469e-9ae6-dcab3a84de43,
  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.},
  author       = {Kozak, M and Jankowska, E and Janowski, R and Grzonka, Z and Grubb, Anders and Alvarez-Fernandez, M and Abrahamson, Magnus and Jaskolski, M},
  issn         = {1399-0047},
  keyword      = {cysteine proteases,protease inhibitors,cystatins,selenomethionyl derivatives},
  language     = {eng},
  number       = {11},
  pages        = {1939--1942},
  publisher    = {International Union of Crystallography},
  series       = {Acta Crystallographica. Section D: Biological Crystallography},
  title        = {Expression of a selenomethionine derivative and preliminary crystallographic studies of human cystatin C},
  url          = {http://dx.doi.org/10.1107/S090744499901121X},
  volume       = {55},
  year         = {1999},
}