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Proceedings Paper

Fluorescence studies of protein crystal nucleation
Author(s): Marc L. Pusey; John Sumida
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Paper Abstract

One of the most powerful and versatile methods for studying molecules in solution is fluorescence. Crystallization typically takes place in a concentrated solution environment, whereas fluorescence typically has an upper concentration limit of approximately 1 X 10-5 M, thus intrinsic fluorescence cannot be employed, but a fluorescent probe must be added to a sub population of the molecules. However the fluorescent species cannot interfere with the self-assembly process. This can be achieved with macromolecules, where fluorescent probes can be covalently attached to a sub population of molecules that are subsequently used to track the system as a whole. We are using fluorescence resonance energy transfer (FRET) to study the initial solution phase self-assembly process of tetragonal lysozyme crystal nucleation, using covalent fluorescent derivatives which crystallize in the characteristic P432121 space group. FRET studies are being carried out between N-terminal lysine bound Texas Red as the donor and N-terminal lysine bound 5-(and-6)- carboxynaphthofluorescein as the acceptor.

Paper Details

Date Published: 29 September 2000
PDF: 10 pages
Proc. SPIE 4098, Optical Devices and Diagnostics in Materials Science, (29 September 2000); doi: 10.1117/12.401612
Show Author Affiliations
Marc L. Pusey, NASA Marshall Space Flight Ctr. (United States)
John Sumida, Universities Space Research Association (United States)


Published in SPIE Proceedings Vol. 4098:
Optical Devices and Diagnostics in Materials Science
David L. Andrews; David L. Andrews; Toshimitsu Asakura; Suganda Jutamulia; Wiley P. Kirk; Max G. Lagally; Ravindra B. Lal; James D. Trolinger, Editor(s)

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