Expression, crystallization and preliminary X-ray studies of the recombinant PTB domain of mouse dok1 protein

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 60; no. 2; pp. 334 - 336
• Main Authors: Shi, Ning, Liu, Yiwei, Ni, Minghao, Yang, MaoJun, Wu, Jing, Peng, Ying, Gao, Feng, Sun, Fei, Peng, Xiaozhong, Qiang, Boqin, Rao, Zihe, Yuan, Jiangang
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.02.2004
• Subjects: Animals; Crystallography, X-Ray - methods; DNA-Binding Proteins - chemistry; dok1 PTB domain; Electrophoresis, Polyacrylamide Gel; Escherichia coli - metabolism; Mice; Models, Molecular; Phosphoproteins - chemistry; Polymerase Chain Reaction; Protein Structure, Tertiary; Recombinant Fusion Proteins - metabolism; Recombinant Proteins - chemistry; RNA-Binding Proteins - chemistry
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444903026696

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 P212121. X‐­ray diffraction data were collected in‐house to 2.5 Å 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 Å resolution at SPring‐8.