Open AccessIn vacuo X‐ray data collection from graphene‐wrapped protein crystals
Author(s) -
Warren Anna J.,
Crawshaw Adam D.,
Trincao Jose,
Aller Pierre,
Alcock Simon,
Nistea Ioana,
Salgado Paula S.,
Evans Gwyndaf
Publication year - 2015
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s1399004715014194
Subject(s) - graphene , protein crystallization , synchrotron , materials science , crystal (programming language) , absorption (acoustics) , diffraction , aqueous solution , x ray , dehydration , crystallography , optics , nanotechnology , analytical chemistry (journal) , chemistry , crystallization , composite material , physics , organic chemistry , biochemistry , computer science , programming language
The measurement of diffraction data from macromolecular crystal samples held in vacuo holds the promise of a very low X‐ray background and zero absorption of incident and scattered beams, leading to better data and the potential for accessing very long X‐ray wavelengths (>3 Å) for native sulfur phasing. Maintaining the hydration of protein crystals under vacuum is achieved by the use of liquid jets, as with serial data collection at free‐electron lasers, or is side‐stepped by cryocooling the samples, as implemented at new synchrotron beamlines. Graphene has been shown to protect crystals from dehydration by creating an extremely thin layer that is impermeable to any exchanges with the environment. Furthermore, owing to its hydrophobicity, most of the aqueous solution surrounding the crystal is excluded during sample preparation, thus eliminating most of the background caused by liquid. Here, it is shown that high‐quality data can be recorded at room temperature from graphene‐wrapped protein crystals in a rough vacuum. Furthermore, it was observed that graphene protects crystals exposed to different relative humidities and a chemically harsh environment.