4E6S

Crystal structure of the SCAN domain from mouse Zfp206

Summary for 4E6S

• Entry DOI: 10.2210/pdb4e6s/pdb
• Related: 1Y7Q 2FI2 3LHR
• Descriptor: Zinc finger and SCAN domain-containing protein 10 (2 entities in total)
• Functional Keywords: scan domain, protein interaction, other scans, n-terminal part, zinc finger transcription factor, transcription
• Biological source: Mus musculus (mouse)
• Total number of polymer chains: 1
• Total formula weight: 10753.48

Authors

Liang, Y.,Choo, S.H.,Rossbach, M.,Baburajendran, N.,Palasingam, P.,Kolatkar, P.R. (deposition date: 2012-03-15, release date: 2012-05-02, Last modification date: 2024-03-20)

Primary citation

Liang, Y.,Choo, S.H.,Rossbach, M.,Baburajendran, N.,Palasingam, P.,Kolatkar, P.R.
Crystal optimization and preliminary diffraction data analysis of the SCAN domain of Zfp206.
Acta Crystallogr.,Sect.F, 68:443-447, 2012

PubMed Abstract: Zfp206 (also named Zscan10) is a transcription factor that plays an important role in maintaining the pluripotent state of embryonic stem cells. Zfp206 is a member of the SCAN-domain family of C(2)H(2) zinc-finger transcription factors. The SCAN domain is a highly conserved motif of 84 residues which mediates the self-association of and heterodimerization between SCAN-domain family transcription factors. The SCAN domain may therefore be the key to the selective oligomerization of and may combinatorially enhance the regulatory versatility of C(2)H(2) zinc fingers. This paper describes crystallization attempts with the SCAN domain of Zfp206 (Zfp206SCAN) and optimization strategies to obtain diffraction-quality crystals. The best diffracting crystal was grown in a solution consisting of 0.3 M ammonium sulfate, 0.1 M Tris-HCl pH 8.6, 25% PEG 3350, 0.1 M ethylenediaminetetraacetic acid disodium salt dehydrate (EDTA) using the hanging-drop vapour-diffusion technique. Optimized crystals diffracted to 1.85 Å resolution and belonged to space group I422, with unit-cell parameters a = 67.57, c = 87.54 Å. A Matthews analysis indicated the presence of one Zfp206SCAN molecule per asymmetric unit.

PubMed: 22505416
DOI: 10.1107/S1744309112006070

Experimental method

X-RAY DIFFRACTION (1.85 Å)