Expression of a selenomethionine derivative and preliminary crystallographic studies of human cystatin C
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1115943
- author
- Kozak, M ; Jankowska, E ; Janowski, R ; Grzonka, Z ; Grubb, Anders LU ; Alvarez-Fernandez, M ; Abrahamson, Magnus LU and Jaskolski, M
- organization
- publishing date
- 1999
- 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
- John Wiley & Sons Inc.
- 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
- 2016-04-01 16:20:38
- date last changed
- 2023-01-04 23:08:17
@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}}, keywords = {{cysteine proteases; protease inhibitors; cystatins; selenomethionyl derivatives}}, language = {{eng}}, number = {{11}}, pages = {{1939--1942}}, publisher = {{John Wiley & Sons Inc.}}, 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}}, doi = {{10.1107/S090744499901121X}}, volume = {{55}}, year = {{1999}}, }