Experimental phase determination with selenomethionine or mercury-derivatization in serial femtosecond crystallography.

ABSTRACT: Serial femtosecond crystallography (SFX) using X-ray free-electron lasers (XFELs) holds enormous potential for the structure determination of proteins for which it is difficult to produce large and high-quality crystals. SFX has been applied to various systems, but rarely to proteins that have previously unknown structures. Consequently, the majority of previously obtained SFX structures have been solved by the molecular replacement method. To facilitate protein structure determination by SFX, it is essential to establish phasing methods that work efficiently for SFX. Here, selenomethionine derivatization and mercury soaking have been investigated for SFX experiments using the high-energy XFEL at the SPring-8 Angstrom Compact Free-Electron Laser (SACLA), Hyogo, Japan. Three successful case

SUBMITTER: Yamashita K 

PROVIDER: S-EPMC5619855 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature