uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Crystallization of a truncated soluble human semicarbazide-sensitive amine oxidase.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
Show others and affiliations
2005 (English)In: Acta Crystallograph Sect F Struct Biol Cryst Commun, ISSN 1744-3091, Vol. 61, no Pt 3, 274-8 p.Article in journal (Refereed) Published
Abstract [en]

Human semicarbazide-sensitive amine oxidase (SSAO) is a homodimeric copper-containing monoamine oxidase that occurs in both a membrane-bound and a soluble form. SSAO is also known as vascular adhesion protein-1 (VAP-1). A truncated soluble form of human SSAO (comprising residues 29-763) was expressed in human embryonic kidney 293 cells and purified to homogeneity. Tetragonal crystals were obtained and a data set extending to 2.5 A was collected. The crystals are merohedrally twinned and the estimation of the twinning fraction was complicated by pseudo-symmetry and the anisotropic character of the crystals. Using a recently developed method for twinning detection that is insensitive to phenomena such as anisotropy or pseudo-symmetry [Padilla & Yeates (2003), Acta Cryst. D59, 1124-1130], the twinning fraction was estimated to be 0.3. The structure was eventually solved by molecular replacement in space group P4(3).

Place, publisher, year, edition, pages
2005. Vol. 61, no Pt 3, 274-8 p.
Keyword [en]
Amine Oxidase (Copper-Containing)/*chemistry/genetics/isolation & purification, Animals, Cell Line, Crystallization, Dimerization, Genetic Vectors, Humans, Kidney/embryology, Mammals, Recombinant Proteins/chemistry/isolation & purification, Sequence Deletion, Transfection, X-Ray Diffraction
Identifiers
URN: urn:nbn:se:uu:diva-21216PubMedID: 16511016OAI: oai:DiVA.org:uu-21216DiVA: diva2:48989
Available from: 2006-12-15 Created: 2006-12-15 Last updated: 2011-01-12

Open Access in DiVA

No full text

Other links

PubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=16511016&dopt=Citation
By organisation
Department of Cell and Molecular BiologyStructural Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

pubmed
urn-nbn

Altmetric score

pubmed
urn-nbn
Total: 345 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf