Crystal optimization and preliminary diffraction data analysis of the SCAN domain of Zfp206

Yu Liang, Siew Hua Choo, Michael Rossbach, Nithya Baburajendran, Paaventhan Palasingam, Prasanna Kolatkar

Research output: Contribution to journalArticle

3 Citations (Scopus)

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 C2H2 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 C2H2 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.

Original languageEnglish
Pages (from-to)443-447
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume68
Issue number4
DOIs
Publication statusPublished - 1 Apr 2012
Externally publishedYes

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Keywords

  • SCAN domain
  • Transcription factors
  • Zfp206

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

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