Serial femtosecond crystallography (SFX) at X-ray free electron lasers (XFELs) has created many new opportunities for protein crystallography, including radiation damage mitigation and the study of dynamics at room temperature. This field is rapidly evolving, requiring new methods of macromolecule organization into diffracting arrays, since current methods of sample preparation and delivery are often the bottleneck which limits productivity. We propose here the LangmuirBlodgett (LB) protein nanofilm technology as a novel approach for direct “on chip” protein molecules organization into the 3D ordered diffracting arrays. The combination of this advanced technology with the XFEL for fixed target SFX has the potential to become an important tool for the structure determination of proteins that are difficult to crystallize, such as membrane proteins of life science interest and with pharmaceutical industry impact

Langmuir-Blodgett Protein Multilayer Nanofilms by XFEL

Pechkova, Eugenia;Nicolini, Claudio
2018-01-01

Abstract

Serial femtosecond crystallography (SFX) at X-ray free electron lasers (XFELs) has created many new opportunities for protein crystallography, including radiation damage mitigation and the study of dynamics at room temperature. This field is rapidly evolving, requiring new methods of macromolecule organization into diffracting arrays, since current methods of sample preparation and delivery are often the bottleneck which limits productivity. We propose here the LangmuirBlodgett (LB) protein nanofilm technology as a novel approach for direct “on chip” protein molecules organization into the 3D ordered diffracting arrays. The combination of this advanced technology with the XFEL for fixed target SFX has the potential to become an important tool for the structure determination of proteins that are difficult to crystallize, such as membrane proteins of life science interest and with pharmaceutical industry impact
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11567/937870
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