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Expression, crystallization and preliminary X-ray studies of the recombinant PTB domain of mouse dok1 protein.
Acta Crystallogr D Biol Crystallogr. 2004 Feb; 60(Pt 2):334-6.AC

Abstract

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.

Authors+Show Affiliations

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.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

14747716

Citation

Shi, Ning, et al. "Expression, Crystallization and Preliminary X-ray Studies of the Recombinant PTB Domain of Mouse Dok1 Protein." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 2, 2004, pp. 334-6.
Shi N, Liu Y, Ni M, et al. Expression, crystallization and preliminary X-ray studies of the recombinant PTB domain of mouse dok1 protein. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 2):334-6.
Shi, N., Liu, Y., Ni, M., Yang, M., Wu, J., Peng, Y., Gao, F., Sun, F., Peng, X., Qiang, B., Rao, Z., & Yuan, J. (2004). Expression, crystallization and preliminary X-ray studies of the recombinant PTB domain of mouse dok1 protein. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 2), 334-6.
Shi N, et al. Expression, Crystallization and Preliminary X-ray Studies of the Recombinant PTB Domain of Mouse Dok1 Protein. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 2):334-6. PubMed PMID: 14747716.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Expression, crystallization and preliminary X-ray studies of the recombinant PTB domain of mouse dok1 protein. AU - Shi,Ning, AU - Liu,Yiwei, AU - Ni,Minghao, AU - Yang,MaoJun, AU - Wu,Jing, AU - Peng,Ying, AU - Gao,Feng, AU - Sun,Fei, AU - Peng,Xiaozhong, AU - Qiang,Boqin, AU - Rao,Zihe, AU - Yuan,Jiangang, Y1 - 2004/01/23/ PY - 2003/08/11/received PY - 2003/11/20/accepted PY - 2004/1/30/pubmed PY - 2004/10/9/medline PY - 2004/1/30/entrez SP - 334 EP - 6 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 2 N2 - 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. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/14747716/Expression_crystallization_and_preliminary_X_ray_studies_of_the_recombinant_PTB_domain_of_mouse_dok1_protein_ DB - PRIME DP - Unbound Medicine ER -