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Robinson, Ian K. Boutet, Sebastien 2015-09-25T20:02:52Z 2015-09-25T20:02:52Z 10000-01-01 2005 2005 The determination of the atomic structure of proteins is very important since much understanding of biological processes cannot be achieved without knowledge of the atomic structure. The preparation of high quality protein crystals suitable for structure determination often proves difficult and even impossible. The technique of coherent x-ray diffraction was used to try to gain a better understanding of protein crystal nucleation and growth. Results are presented along with technical difficulties arising from radiation damage. The results reveal the presence of surface strain in micron-sized protein crystals. Studies of nucleation at low temperature were performed along with simulations. The analysis revealed that isotropic nucleation was the main pathway but that nucleation also proceeds in a more planar fashion in some cases. Made available in DSpace on 2015-09-25T20:02:52Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3198932.pdf: 4301357 bytes, checksum: 34875c1b8707e18757b89f0736bbde6e (MD5) Previous issue date: 2005 Embargo set by: Seth Robbins for item 81799 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 145 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2005. http://hdl.handle.net/2142/80517 (MiAaPQ)AAI3198932 eng Biophysics, General Coherent X -Ray Diffractive Imaging and Nucleation of Protein Crystals text Physics Physics University of Illinois at Urbana-Champaign Dissertation Ph.D.