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- All Subjects: LCP
- Creators: Schmidt, Kevin
Description
ABSTRACT
X-Ray crystallography and NMR are two major ways of achieving atomic
resolution of structure determination for macro biomolecules such as proteins. Recently, new developments of hard X-ray pulsed free electron laser XFEL opened up new possibilities to break the dilemma of radiation dose and spatial resolution in diffraction imaging by outrunning radiation damage with ultra high brightness femtosecond X-ray pulses, which is so short in time that the pulse terminates before atomic motion starts. A variety of experimental techniques for structure determination of macro biomolecules is now available including imaging of protein nanocrystals, single particles such as viruses, pump-probe experiments for time-resolved nanocrystallography, and snapshot wide- angle x-ray scattering (WAXS) from molecules in solution. However, due to the nature of the "diffract-then-destroy" process, each protein crystal would be destroyed once
probed. Hence a new sample delivery system is required to replenish the target crystal at a high rate. In this dissertation, the sample delivery systems for the application of XFELs to biomolecular imaging will be discussed and the severe challenges related to the delivering of macroscopic protein crystal in a stable controllable way with minimum waste of sample and maximum hit rate will be tackled with several different development of injector designs and approaches. New developments of the sample delivery system such as liquid mixing jet also opens up new experimental methods which gives opportunities to study of the chemical dynamics in biomolecules in a molecular structural level. The design and characterization of the system will be discussed along with future possible developments and applications. Finally, LCP injector will be discussed which is critical for the success in various applications.
X-Ray crystallography and NMR are two major ways of achieving atomic
resolution of structure determination for macro biomolecules such as proteins. Recently, new developments of hard X-ray pulsed free electron laser XFEL opened up new possibilities to break the dilemma of radiation dose and spatial resolution in diffraction imaging by outrunning radiation damage with ultra high brightness femtosecond X-ray pulses, which is so short in time that the pulse terminates before atomic motion starts. A variety of experimental techniques for structure determination of macro biomolecules is now available including imaging of protein nanocrystals, single particles such as viruses, pump-probe experiments for time-resolved nanocrystallography, and snapshot wide- angle x-ray scattering (WAXS) from molecules in solution. However, due to the nature of the "diffract-then-destroy" process, each protein crystal would be destroyed once
probed. Hence a new sample delivery system is required to replenish the target crystal at a high rate. In this dissertation, the sample delivery systems for the application of XFELs to biomolecular imaging will be discussed and the severe challenges related to the delivering of macroscopic protein crystal in a stable controllable way with minimum waste of sample and maximum hit rate will be tackled with several different development of injector designs and approaches. New developments of the sample delivery system such as liquid mixing jet also opens up new experimental methods which gives opportunities to study of the chemical dynamics in biomolecules in a molecular structural level. The design and characterization of the system will be discussed along with future possible developments and applications. Finally, LCP injector will be discussed which is critical for the success in various applications.
ContributorsWang, Dingjie (Author) / Spence, John CH (Thesis advisor) / Weierstall, Uwe (Committee member) / Schmidt, Kevin (Committee member) / Fromme, Petra (Committee member) / Ozkan, Banu (Committee member) / Arizona State University (Publisher)
Created2014
Description
Seeking an upper limit of the Neutron Electric Dipole Moment (nEDM) is a test of charge-parity (CP) violation beyond the Standard Model. The present experimentally tested nEDM upper limit is 3x10^(26) e cm. An experiment to be performed at the Oak Ridge National Lab Spallation Neutron Source (SNS) facility seeks to reach the 3x10^(28) e cm limit. The experiment is designed to probe for a dependence of the neutron's Larmor precession frequency on an applied electric eld. The experiment will use polarized helium-3
(3He) as a comagnetometer, polarization analyzer, and detector.
Systematic influences on the nEDM measurement investigated in this thesis include (a) room temperature measurements on polarized 3He in a measurement cell made from the same materials as the nEDM experiment, (b) research and development of the Superconducting QUantum Interference Devices (SQUID) which will be used in the nEDM experiment, (c) design contributions for an experiment with nearly all the same conditions as will be present in the nEDM experiment, and (d) scintillation studies in superfluid helium II generated from alpha particles which are fundamentally similar to the nEDM scintillation process. The result of this work are steps toward achievement of a new upper limit for the nEDM experiment at the SNS facility.
(3He) as a comagnetometer, polarization analyzer, and detector.
Systematic influences on the nEDM measurement investigated in this thesis include (a) room temperature measurements on polarized 3He in a measurement cell made from the same materials as the nEDM experiment, (b) research and development of the Superconducting QUantum Interference Devices (SQUID) which will be used in the nEDM experiment, (c) design contributions for an experiment with nearly all the same conditions as will be present in the nEDM experiment, and (d) scintillation studies in superfluid helium II generated from alpha particles which are fundamentally similar to the nEDM scintillation process. The result of this work are steps toward achievement of a new upper limit for the nEDM experiment at the SNS facility.
ContributorsDipert, Robert (Author) / Alarcon, Ricardo (Thesis advisor) / Chamberlin, Ralph (Committee member) / Golub, Robert (Committee member) / Chen, Tingyong (Committee member) / Schmidt, Kevin (Committee member) / Arizona State University (Publisher)
Created2019