title: Crystallization and preliminary X-ray diffraction analysis of the dimerization domain of the tumour suppressor ING4.
abstract: Inhibitor of growth protein 4 (ING4) belongs to the ING family of tumour suppressors and is involved in chromatin remodelling, in growth arrest and, in cooperation with p53, in senescence and apoptosis. Whereas the structure and histone H3-binding properties of the C-terminal PHD domains of the ING proteins are known, no structural information is available for the N-terminal domains. This domain contains a putative oligomerization site rich in helical structure in the ING2-5 members of the family. The N-terminal domain of ING4 was overexpressed in Escherichia coli and purified to homogeneity. Crystallization experiments yielded crystals that were suitable for high-resolution X-ray diffraction analysis. The crystals belonged to the orthorhombic space group C222, with unit-cell parameters a = 129.7, b = 188.3, c = 62.7 A. The self-rotation function and the Matthews coefficient suggested the presence of three protein dimers per asymmetric unit. The crystals diffracted to a resolution of 2.3 A using synchrotron radiation at the Swiss Light Source (SLS) and the European Synchrotron Radiation Facility (ESRF).
authors.affiliation: Structural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, Edificio 800, 48160 Derio, Spain.
authors.forename: Simone
authors.initials: S
authors.lastname: Culurgioni
authors.forename: Inés G
authors.initials: IG
authors.lastname: Muñoz
authors.forename: Alicia
authors.initials: A
authors.lastname: Palacios
authors.forename: Pilar
authors.initials: P
authors.lastname: Redondo
authors.forename: Francisco J
authors.initials: FJ
authors.lastname: Blanco
authors.forename: Guillermo
authors.initials: G
authors.lastname: Montoya
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D025521:Tumor Suppressor Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D025521:Tumor Suppressor Proteins
references.citation: Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):72-82
references.pmid: 16369096
references.citation: J Biol Chem. 2008 Jun 6;283(23):15956-64
references.pmid: 18381289
references.citation: Trends Biochem Sci. 2007 Nov;32(11):509-19
references.pmid: 17949986
references.citation: FEBS Lett. 2006 Dec 22;580(30):6903-8
references.pmid: 17157298
references.citation: Cell. 2006 Jul 14;126(1):22-4
references.pmid: 16839870
references.citation: Mol Cell. 2009 Jan 30;33(2):248-56
references.pmid: 19187765
references.citation: Trends Biochem Sci. 2006 Jan;31(1):35-40
references.pmid: 16297627
references.citation: J Mol Biol. 2010 Mar 5;396(4):1117-27
references.pmid: 20053357
references.citation: Mol Biol Evol. 2005 Jan;22(1):104-16
references.pmid: 15356280
references.citation: Int J Cancer. 2008 Oct 1;123(7):1483-90
references.pmid: 18636562
references.citation: Mol Cell Biol. 2008 Jan;28(1):140-53
references.pmid: 17954561
references.citation: Mol Cell Biol. 2000 Jun;20(11):3807-16
references.pmid: 10805724
references.citation: Mol Cell. 2006 Jan 6;21(1):51-64
references.pmid: 16387653