Literature DB >> 19153449

Crystallization and preliminary X-ray diffraction analysis of GCIP/HHM transcriptional regulator.

Azusa Seto1, Hiroaki Ikushima, Toshiyasu Suzuki, Yusuke Sato, Shuya Fukai, Keiko Yuki, Keiji Miyazawa, Kohei Miyazono, Ryuichiro Ishitani, Osamu Nureki.   

Abstract

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 A resolution. Preliminary phase calculations using the data set obtained from the SeMet crystal suggested that the crystal belonged to space group P3(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.

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Year:  2008        PMID: 19153449      PMCID: PMC2628855          DOI: 10.1107/S1744309108038219

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  13 in total

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