%0 Thesis
%A Roedig, Philip
%T A New Fixed-Target Approach for Serial Crystallography at Synchrotron Light Sources and X-ray Free Electron Lasers
%N DESY-THESIS-2017-027
%I Universität Hamburg
%V Dr.
%C Hamburg
%M PUBDB-2017-07483
%M DESY-THESIS-2017-027
%B DESY-THESIS
%P 185
%D 2017
%Z Universität Hamburg, Diss., 2016
%X In the framework of this thesis, a new method for high-speed fixed-target serial crystallography experiments and its applicability to biomacromolecular crystallography at both synchrotron light sources and X-ray free electron lasers (XFELs) is presented. The method is based on a sample holder, which can carry up to 20,000 microcrystals and which is made of single-crystalline silicon. Using synchrotron radiation, the structure of Operophtera brumata cytoplasmic polyhedrosis virus type 18 polyhedrin, lysozyme and cubic insulin was determined by collecting X-ray diffraction data from multiple microcrystals. Data collection was shown to be possible at both cryogenic and ambient conditions. For room-temperature measurements, both global and specific indications of radiation damage were investigated and characterized. Due to the sieve-like structure of the chip, the microcrystals tend to arrange themselves according to the micropore pattern, which allows for efficient sampling of the sample material. In combination with a high-speed scanning stage, the sample holder was furthermore shown to be highly suitable for serial femtosecond crystallography experiments. By fast raster scanning of the chip through the pulsed X-ray beam of an XFEL, structure determination of a virus, using the example of bovine enterovirus type 2, has been demonstrated at an XFEL for the first time. Hit rates of up to 100
%F PUB:(DE-HGF)3 ; PUB:(DE-HGF)29 ; PUB:(DE-HGF)11
%9 BookReportDissertation / PhD Thesis
%R 10.3204/PUBDB-2017-07483
%U https://bib-pubdb1.desy.de/record/331060