Attenuated total reflection-FT-IR spectroscopic imaging of protein crystallization


Protein crystallization is of strategic and commercial relevance in the post-genomic era because of its pivotal role in structural proteomics projects. Although protein structures are crucial for understanding the function of proteins and to the success of rational drug design and other biotechnology applications, obtaining high quality crystals is a major bottleneck to progress. The major means of obtaining crystals is by massive-scale screening of a target protein solution with numerous crystallizing agents. However, when crystals appear in these screens, one cannot easily know if they are crystals of protein, salt, or any other molecule that happens to be present in the trials. We present here a method based on Attenuated Total Reflection (ATR)-FT-IR imaging that reliably identifies protein crystals through a combination of chemical specificity and the visualizing capability of this approach, thus solving a major hurdle in protein crystallization. ATR-FT-IR imaging was successfully applied to study the crystallization of thaumatin and lysozyme in a high-throughput manner, simultaneously from six different solutions. This approach is fast as it studies protein crystallization in situ and provides an opportunity to examine many different samples under a range of conditions.

Publication DOI:
Divisions: College of Health & Life Sciences > School of Biosciences
College of Health & Life Sciences
College of Health & Life Sciences > School of Biosciences > Cellular and Molecular Biomedicine
Additional Information: © 2009 American Chemical Society. This document is the Accepted Manuscript version of a Published Work that appeared in final form in Analytical Chemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see
Uncontrolled Keywords: protein crystallization,post-genomic era,structural proteomics projects,rational drug design,Analytical Chemistry
Publication ISSN: 1520-6882
Last Modified: 15 Apr 2024 07:09
Date Deposited: 19 Jul 2010 14:00
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Related URLs: http://www.scop ... tnerID=8YFLogxK (Scopus URL)
http://pubs.acs ... .1021/ac900455y (Publisher URL)
PURE Output Type: Article
Published Date: 2009-05-23
Authors: Chan, K. L. Andrew
Govada, Lata
Bill, Roslyn M. (ORCID Profile 0000-0003-1331-0852)
Chayen, Naomi E.
Kazarian, Sergei G.



Version: Accepted Version

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