Open AccessOverproduction, purification, crystallization and preliminary X‐ray diffraction studies of the human spliceosomal protein TXNL4B
Author(s) -
Jin Tengchuan,
Howard Andrew J.,
Golemis Erica A.,
Wang Yingtong,
Zhang YuZhu
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105002861
Subject(s) - crystallization , overproduction , crystallography , x ray , x ray crystallography , diffraction , materials science , chemistry , physics , biochemistry , optics , organic chemistry , gene
The human gene coding for the spliceosomal protein thioredoxin‐like 4B (TXNL4B) was overexpressed in Escherichia coli and the encoded protein was purified and crystallized. Well diffracting single crystals were obtained by the vapor‐diffusion method in hanging drops. The crystals belong to the primitive monoclinic space group P 2, with unit‐cell parameters a = 39.0, b = 63.6, c = 51.0 Å, β = 92.484°, and diffract to at least 1.50 Å. A SeMet derivative of the protein was prepared and crystallized for MAD phasing.