Utilize este identificador para referenciar este registo: https://hdl.handle.net/10216/108246
Autor(es): Meyer, P
Socias, S
Key, J
Ransey, E
Tjon, E
Buschiazzo, A
Lei, M
Botka, C
Withrow, J
Neau, D
Rajashankar, K
Anderson, K
Baxter, R
Blacklow, S
Boggon, T
Bonvin, A
Borek, D
Brett, T
Caflisch, A
Chang, C
Chazin, W
Corbett, K
Cosgrove, M
Crosson, S
Dhe-Paganon, S
Di Cera, E
Drennan, C
Eck, M
Eichman, B
Fan, Q
Ferré-D'Amaré, A
Fromme, J
Garcia, K
Gaudet, R
Gong, P
Harrison, S
Heldwein, E
Jia, Z
Keenan, R
Kruse, A
Kvansakul, M
McLellan, J
Modis, Y
Nam, Y
Otwinowski, Z
Pai, E
Pereira, PJ
Petosa, C
Raman, C
Rapoport, T
Roll-Mecak, A
Rosen, M
Rudenko, G
Schlessinger, J
Schwartz, T
Shamoo, Y
Sondermann, H
Tao, Y
Tolia, N
Tsodikov, O
Westover, K
Wu, H
Foster, I
Fraser, J
Maia, F
Gonen, T
Kirchhausen, T
Diederichs, K
Crosas, M
Sliz, P
Título: Data publication with the structural biology data grid supports live analysis
Editor: Nature Publishing Group
Data de publicação: 2016
Resumo: Access to experimental X-ray diffraction image data is fundamental for validation and reproduction of macromolecular models and indispensable for development of structural biology processing methods. Here, we established a diffraction data publication and dissemination system, Structural Biology Data Grid (SBDG; data. sbgrid. org), to preserve primary experimental data sets that support scientific publications. Data sets are accessible to researchers through a community driven data grid, which facilitates global data access. Our analysis of a pilot collection of crystallographic data sets demonstrates that the information archived by SBDG is sufficient to reprocess data to statistics that meet or exceed the quality of the original published structures. SBDG has extended its services to the entire community and is used to develop support for other types of biomedical data sets. It is anticipated that access to the experimental data sets will enhance the paradigm shift in the community towards a much more dynamic body of continuously improving data analysis.
Assunto: X-ray scattering
Protein data-bank
Macromolecular crystallography
Structure models
Data quality
Synchrotron
Software
Science
Experiences
Resolution
DOI: 10.1038/ncomms10882
URI: http://hdl.handle.net/10216/108246
Fonte: Nature Communications, vol. 7:10882
Tipo de Documento: Artigo em Revista Científica Internacional
Condições de Acesso: openAccess
Licença: http://creativecommons.org/licenses/by/4.0/
Aparece nas coleções:I3S - Artigo em Revista Científica Internacional

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