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Hydroxyethyl cellulose matrix applied to serial crystallography.

Michihiro SugaharaTakanori NakaneTetsuya MasudaMamoru SuzukiShigeyuki InoueChangyong SongRie TanakaToru NakatsuEiichi MizohataFumiaki YumotoKensuke TonoYasumasa JotiTakashi KameshimaTakaki HatsuiMakina YabashiOsamu NurekiKeiji NumataEriko NangoSo Iwata
Published in: Scientific reports (2017)
Serial femtosecond crystallography (SFX) allows structures of proteins to be determined at room temperature with minimal radiation damage. A highly viscous matrix acts as a crystal carrier for serial sample loading at a low flow rate that enables the determination of the structure, while requiring consumption of less than 1 mg of the sample. However, a reliable and versatile carrier matrix for a wide variety of protein samples is still elusive. Here we introduce a hydroxyethyl cellulose-matrix carrier, to determine the structure of three proteins. The de novo structure determination of proteinase K from single-wavelength anomalous diffraction (SAD) by utilizing the anomalous signal of the praseodymium atom was demonstrated using 3,000 diffraction images.
Keyphrases
  • room temperature
  • ionic liquid
  • oxidative stress
  • solid phase extraction
  • deep learning
  • crystal structure
  • molecular dynamics
  • machine learning
  • radiation therapy
  • silver nanoparticles
  • electron microscopy