Crystallization and preliminary X-ray diffraction analysis of GCIP/HHM transcriptional regulator.
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.
Seto
Azusa
A
Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Yokohama-shi, Kanagawa, Japan.
Ikushima
Hiroaki
H
Suzuki
Toshiyasu
T
Sato
Yusuke
Y
Fukai
Shuya
S
Yuki
Keiko
K
Miyazawa
Keiji
K
Miyazono
Kohei
K
Ishitani
Ryuichiro
R
Nureki
Osamu
O
D049109:Cell Proliferation; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D004247:DNA / Q000737:chemistry; D006801:Humans; D011485:Protein Binding; D012645:Selenomethionine / Q000737:chemistry; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism; D014158:Transcription, Genetic; D016212:Transforming Growth Factor beta / Q000378:metabolism; D014961:X-Ray Diffraction / Q000379:methods
C485815:CCNDBP1 protein, human; D014157:Transcription Factors; D016212:Transforming Growth Factor beta; D004247:DNA; D012645:Selenomethionine