Open AccessCrystallization and preliminary X‐ray diffraction analysis of GCIP/HHM transcriptional regulator
Author(s) -
Seto Azusa,
Ikushima Hiroaki,
Suzuki Toshiyasu,
Sato Yusuke,
Fukai Shuya,
Yuki Keiko,
Miyazawa Keiji,
Miyazono Kohei,
Ishitani Ryuichiro,
Nureki Osamu
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108038219
Subject(s) - crystallization , regulator , x ray , crystallography , diffraction , x ray crystallography , transcriptional regulation , chemistry , materials science , biophysics , microbiology and biotechnology , biology , biochemistry , gene , physics , transcription factor , optics , organic chemistry
GCIP/HHM is a human nuclear protein that is implicated in regulation of cell proliferation. Its primary structure contains helix–loop–helix and leucine‐zipper motifs but lacks a DNA‐binding basic region. Native and selenomethionine‐derivatized (SeMet) crystals of full‐length GCIP/HHM were obtained using the hanging‐drop vapour‐diffusion method. The crystals were greatly improved by adding tris(2‐carboxyethyl)phosphine as a reducing reagent and diffracted to 3.5 Å resolution. Preliminary phase calculations using the data set obtained from the SeMet crystal suggested that the crystal belonged to space group P 3 2 21 and contained one molecule per asymmetric unit. Structure determination by the multiple‐wavelength anomalous dispersion method using the SeMet crystals is in progress.