Native sulfur/chlorine SAD phasing for serial femtosecond crystallography

Serial femtosecond crystallography (SFX) allows structures to be determined with minimal radiation damage. However, phasing native crystals in SFX is not very common. Here, the structure determination of native lysozyme from single-wavelength anomalous diffraction (SAD) by utilizing the anomalous si...

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Detalles Bibliográficos
Autores principales: Nakane, Takanori, Song, Changyong, Suzuki, Mamoru, Nango, Eriko, Kobayashi, Jun, Masuda, Tetsuya, Inoue, Shigeyuki, Mizohata, Eiichi, Nakatsu, Toru, Tanaka, Tomoyuki, Tanaka, Rie, Shimamura, Tatsuro, Tono, Kensuke, Joti, Yasumasa, Kameshima, Takashi, Hatsui, Takaki, Yabashi, Makina, Nureki, Osamu, Iwata, So, Sugahara, Michihiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2015
Materias:
Research Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4667287/
https://www.ncbi.nlm.nih.gov/pubmed/26627659
http://dx.doi.org/10.1107/S139900471501857X
Descripción
Sumario:Serial femtosecond crystallography (SFX) allows structures to be determined with minimal radiation damage. However, phasing native crystals in SFX is not very common. Here, the structure determination of native lysozyme from single-wavelength anomalous diffraction (SAD) by utilizing the anomalous signal of sulfur and chlorine at a wavelength of 1.77 Å is successfully demonstrated. This sulfur SAD method can be applied to a wide range of proteins, which will improve the determination of native crystal structures.

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