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        <identifier>oai:www.ideals.illinois.edu:2142/82410</identifier>
        <datestamp>2023-07-11</datestamp>
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        <thesis xmlns="http://www.ndltd.org/standards/metadata/etdms/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:dc="http://purl.org/dc/elements/1.1/" xsi:schemaLocation="http://www.ndltd.org/standards/metadata/etdms/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdms11.xsd http://purl.org/dc/elements/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdmsdc.xsd">
          <dc:contributor>Kenis, Paul J.A.</dc:contributor>
          <dc:creator>Talreja, Sameer</dc:creator>
          <dc:date>2015-09-25T20:43:37Z</dc:date>
          <dc:date>2015-09-25T20:43:37Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>2008</dc:date>
          <dc:date>2008</dc:date>
          <dc:description>In sum, we report new evaporation- and dilution-based protocols that will enable structural biologist to rapidly determine the phase diagram (e.g. solubility boundary, metastable zone width) of proteins of unknown structure using a very small sample volume. The knowledge of phase diagram of a protein/precipitant system thus obtained will be useful in obtaining high quality crystals for X-ray diffraction studies. Moreover, we use theory to compare different protein molecules on a generalized phase diagram using the solubility data obtained from our experiments. The comparison of the solubility boundary and the metastable boundary on the same footing will provide a reasonable estimate of the metastable zone width, which will aid crystallographers in screening conditions conducive for protein crystallization. We also develop a kinetic model that describes the competition between the rates of supersaturation, crystal nucleation and crystal growth occurring in the regulated-evaporation crystallization process. The knowledge of these rates coupled with the knowledge of the phase diagram of a protein/precipitant system will enable crystallographers to predict  a priori the outcome of an experiment performed in an evaporation-based crystallization platform.</dc:description>
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  Previous issue date: 2008</dc:description>
          <dc:description>Embargo set by: Seth Robbins for item 83691
Lift date: Forever
Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>U of I Only</dc:description>
          <dc:description>139 p.</dc:description>
          <dc:description>Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2008.</dc:description>
          <dc:identifier>http://hdl.handle.net/2142/82410</dc:identifier>
          <dc:identifier>(MiAaPQ)AAI3314911</dc:identifier>
          <dc:language>eng</dc:language>
          <dc:subject>Engineering, Chemical</dc:subject>
          <dc:title>Elucidation of Protein -Precipitant Phase Diagrams and Their Link to Crystal Quality</dc:title>
          <dc:type>text</dc:type>
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            <department>Chemical Engineering</department>
            <discipline>Chemical Engineering</discipline>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
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