Expression, crystallization and preliminary X-ray studies of the recombinant PTB domain of mouse dok1 protein.
The PTB domain of mouse dok1 fusion protein has been overexpressed in Escherichia coli and crystallized in a form suitable for X-ray crystallographic study. Crystals have been obtained using the vapour-diffusion method and belong to space group P2(1)2(1)2(1). X-ray diffraction data were collected in-house to 2.5 A resolution. A selenomethionine (SeMet) dok1 PTB fusion-protein derivative was expressed using the same expression system, purified in a reductive environment and crystals were obtained under similar conditions. Subsequently, three different wavelength data sets from the derivative crystal were collected to 2.5 A resolution at SPring-8.
Shi
Ning
N
National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences, Peking Union Medical College, National Human Genome Center, Beijing 100005, People's Republic of China.
Liu
Yiwei
Y
Ni
Minghao
M
Yang
MaoJun
M
Wu
Jing
J
Peng
Ying
Y
Gao
Feng
F
Sun
Fei
F
Peng
Xiaozhong
X
Qiang
Boqin
B
Rao
Zihe
Z
Yuan
Jiangang
J
D000818:Animals; D018360:Crystallography, X-Ray / Q000379:methods*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D051379:Mice; D008958:Models, Molecular; D010750:Phosphoproteins / Q000737:chemistry*; D016133:Polymerase Chain Reaction; D017434:Protein Structure, Tertiary; D016601:RNA-Binding Proteins / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry*
D004268:DNA-Binding Proteins; C489561:Dok1 protein, mouse; C074561:GAP-associated protein p62; D010750:Phosphoproteins; D016601:RNA-Binding Proteins; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins