title: Crystallization and calcium/sulfur SAD phasing of the human EF-hand protein S100A2.
abstract: Human S100A2 is an EF-hand protein and acts as a major tumour suppressor, binding and activating p53 in a Ca2+-dependent manner. Ca2+-bound S100A2 was crystallized and its structure was determined based on the anomalous scattering provided by six S atoms from methionine residues and four calcium ions present in the asymmetric unit. Although the diffraction data were recorded at a wavelength of 0.90 A, which is usually not assumed to be suitable for calcium/sulfur SAD, the anomalous signal was satisfactory. A nine-atom substructure was determined at 1.8 A resolution using SHELXD, and SHELXE was used for density modification and phase extension to 1.3 A resolution. The electron-density map obtained was well interpretable and could be used for automated model building by ARP/wARP.
authors.affiliation: Department of Biology, University of Konstanz, Postfach M665, Universitätsstrasse 10, 78457 Konstanz, Germany.
authors.forename: Michael
authors.initials: M
authors.lastname: Koch
authors.forename: Joachim
authors.initials: J
authors.lastname: Diez
authors.forename: Armin
authors.initials: A
authors.lastname: Wagner
authors.forename: Günter
authors.initials: G
authors.lastname: Fritz
mesh_terms: D002118:Calcium / Q000737:chemistry*; D002630:Chemotactic Factors / Q000737:chemistry*; D018360:Crystallography, X-Ray; D020832:EF Hand Motifs; D006801:Humans; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D009418:S100 Proteins / Q000737:chemistry*; D013455:Sulfur / Q000737:chemistry*
chemical_list: D002630:Chemotactic Factors; D009418:S100 Proteins; C098997:S100A2 protein, human; D013455:Sulfur; D002118:Calcium
references.citation: Nature. 1981 Mar 12;290(5802):107-113
references.pmid: 28769131
references.citation: Biochem Biophys Res Commun. 2004 Oct 1;322(4):1111-22
references.pmid: 15336958
references.citation: Nat Protoc. 2008;3(7):1171-9
references.pmid: 18600222
references.citation: Biochim Biophys Acta. 2007 Mar;1773(3):457-70
references.pmid: 17239974
references.citation: Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501
references.pmid: 20383002
references.citation: Protein Sci. 2008 Oct;17(10):1663-70
references.pmid: 18694925
references.citation: Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2825-9
references.pmid: 1849277
references.citation: Nat Struct Biol. 1999 May;6(5):458-63
references.pmid: 10331874
references.citation: Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):96-101
references.pmid: 16369098
references.citation: J Biol Chem. 2009 May 15;284(20):13804-13811
references.pmid: 19297317
references.citation: Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):247-55
references.pmid: 10089417
references.citation: Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55
references.pmid: 15299926
references.citation: Bioinformatics. 2004 Sep 22;20(14):2162-8
references.pmid: 14871873
references.citation: Biochim Biophys Acta. 2006 Nov;1763(11):1282-3
references.pmid: 16938360
references.citation: J Cell Sci. 1998 Jul 30;111 ( Pt 14):2043-54
references.pmid: 9645951
references.citation: EMBO J. 2007 Aug 22;26(16):3868-78
references.pmid: 17660747
references.citation: Acta Crystallogr A. 1991 Mar 1;47 ( Pt 2):110-9
references.pmid: 2025413
references.citation: J Mol Biol. 2008 May 9;378(4):933-42
references.pmid: 18394645
references.citation: Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt 11):1120-3
references.pmid: 17077493
references.citation: Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
references.pmid: 15572765
references.citation: Proc Natl Acad Sci U S A. 2005 Mar 29;102(13):4735-40
references.pmid: 15781852
references.citation: Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):125-32
references.pmid: 20124692
references.citation: J Mol Biol. 2007 Jul 27;370(5):887-98
references.pmid: 17553524
references.citation: Acta Crystallogr A. 2008 Jan;64(Pt 1):112-22
references.pmid: 18156677
references.citation: J Biol Chem. 2005 Aug 12;280(32):29186-93
references.pmid: 15941720