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In-situ and real-time growth observation of high-quality protein crystals under quasi-microgravity on earth

Precise protein structure determination provides significant information on life science research, although high-quality crystals are not easily obtained. We developed a system for producing high-quality protein crystals with high throughput. Using this system, gravity-controlled crystallization are...

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Detalles Bibliográficos
Autores principales: Nakamura, Akira, Ohtsuka, Jun, Kashiwagi, Tatsuki, Numoto, Nobutaka, Hirota, Noriyuki, Ode, Takahiro, Okada, Hidehiko, Nagata, Koji, Kiyohara, Motosuke, Suzuki, Ei-ichiro, Kita, Akiko, Wada, Hitoshi, Tanokura, Masaru
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4768258/
https://www.ncbi.nlm.nih.gov/pubmed/26916802
http://dx.doi.org/10.1038/srep22127
Descripción
Sumario:Precise protein structure determination provides significant information on life science research, although high-quality crystals are not easily obtained. We developed a system for producing high-quality protein crystals with high throughput. Using this system, gravity-controlled crystallization are made possible by a magnetic microgravity environment. In addition, in-situ and real-time observation and time-lapse imaging of crystal growth are feasible for over 200 solution samples independently. In this paper, we also report results of crystallization experiments for two protein samples. Crystals grown in the system exhibited magnetic orientation and showed higher and more homogeneous quality compared with the control crystals. The structural analysis reveals that making use of the magnetic microgravity during the crystallization process helps us to build a well-refined protein structure model, which has no significant structural differences with a control structure. Therefore, the system contributes to improvement in efficiency of structural analysis for “difficult” proteins, such as membrane proteins and supermolecular complexes.