Crystallization of the actin-binding domain of human alpha-actinin: analysis of microcrystals of SeMet-labelled protein
2003 (English)In: Acta Crystallographica Section D: Biological Crystallography, ISSN 0907-4449, E-ISSN 1399-0047, Vol. 59, no Pt 4, 724-726 p.Article in journal (Refereed) Published
Alpha-actinin forms antiparallel homodimers that cross-link actin filaments from adjacent sarcomeres within the Z-discs of striated muscle. The N-terminal actin-binding domain (ABD) is composed of two calponin homology (CH) domains followed by four spectrin-like repeats and a calmodulin-like EF-hand domain at the C-terminus. The ABD of human alpha-actinin crystallizes in space group P2(1), with unit-cell parameters a = 101.9, b = 38.4, c = 154.9 A, beta = 109.2 degrees. A complete native data set from a native crystal was collected extending to 2.0 A resolution and a single-wavelength anomalous dispersion (SAD) data set to 2.9 A resolution was collected from a selenomethionine-labelled microcrystal using the microfocusing beamline ID-13 at the ESRF. Analysis of the anomalous contribution shows a rapid decrease in the sigma(normal)/sigma(anomal) ratio owing to radiation damage.
Place, publisher, year, edition, pages
Blackwell Munksgaard, 2003. Vol. 59, no Pt 4, 724-726 p.
Actinin/*chemistry/isolation & purification/metabolism, Actins/*metabolism, Cloning; Molecular, Crystallization, Humans, Indicators and Reagents, Protein Binding, Selenomethionine/chemistry
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
IdentifiersURN: urn:nbn:se:umu:diva-13968DOI: 10.1107/S0907444903002063ISI: 000181815600015PubMedID: 12657793OAI: oai:DiVA.org:umu-13968DiVA: diva2:153639