Open AccessCrystal optimization and preliminary diffraction data analysis of the SCAN domain of Zfp206
Author(s) -
Liang Yu,
Choo Siew Hua,
Rossbach Michael,
Baburajendran Nithya,
Palasingam Paaventhan,
Kolatkar Prasanna R
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112006070
Subject(s) - crystallography , crystallization , ammonium sulfate , zinc finger , chemistry , diffraction , molecule , transcription factor , gene , biochemistry , organic chemistry , physics , optics
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 I 422, with unit‐cell parameters a = 67.57, c = 87.54 Å. A Matthews analysis indicated the presence of one Zfp206SCAN molecule per asymmetric unit.