Open AccessCrystallization and preliminary X‐ray crystallographic analysis of Salmonella Typhimurium CueP
Author(s) -
Yun BoYoung,
Piao Shunfu,
Kim YeonGil,
Moon Hyung Ryong,
Choi Eun Joo,
Kim YoungOk,
Nam BoHye,
Lee SangJun,
Ha NamChul
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111010645
Subject(s) - crystallization , crystallography , salmonella , materials science , x ray , x ray crystallography , chemistry , biology , physics , bacteria , diffraction , genetics , optics , organic chemistry
Salmonella enterica serovar Typhimurium ( S. Typhimurium) can survive in the phagosome of macrophages, causing serious medical and veterinary problems. CueP is uniquely found in S. Typhimurium and has been characterized as a major periplasmic copper‐binding protein. Although cueP has been identified as being responsible for the copper resistance of the bacterium in vivo , the biochemical role and three‐dimensional structure of CueP remain unknown. In this study, CueP from S. Typhimurium was overexpressed and the recombinant protein was purified using Ni–NTA affinity, anion‐exchange and gel‐filtration chromatographies. The purified CueP protein was crystallized using the vapour‐diffusion method. A diffraction data set was collected to 2.5 Å resolution at 100 K. The crystal belonged to space group P 2 1 2 1 2 1 . To obtain initial phases, selenomethionyl‐substituted protein was overproduced and purified. Optimization of crystallization conditions for the selenomethionyl‐substituted protein is in progress.