
Preliminary X‐ray crystallographic studies of the short form of the human TRAF4 TRAF domain
Author(s) -
Yoon Jong Hwan,
Park Hyun Ho
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113019179
Subject(s) - crystallography , hexagonal crystal system , domain (mathematical analysis) , x ray , materials science , biology , chemistry , physics , optics , mathematical analysis , mathematics
TNF (tumour necrosis factor) receptor‐associated factor 4 (TRAF4) is a unique TRAF protein that participates in morphogenetic and developmental function and cell migration. TRAF‐family proteins contain a TRAF domain for target interaction. In this study, the short form of the human TRAF4 TRAF domain, corresponding to amino acids 290–462, was overexpressed in Escherichia coli using engineered C‐terminal His tags. The short form of the TRAF4 TRAF domain was purified to homogeneity and crystallized at 293 K. Finally, X‐ray diffraction data were collected to a resolution of 4.2 Å from a crystal belonging to the hexagonal space group P 3 2 , with unit‐cell parameters a = b = 147.17, c = 202.69 Å.