Fluorescence studies of protein crystal nucleation

Marc L. Pusey; John Sumida

doi:10.1117/12.401612

29 September 2000 Fluorescence studies of protein crystal nucleation

Marc L. Pusey, John Sumida

Proceedings Volume 4098, Optical Devices and Diagnostics in Materials Science; (2000) https://doi.org/10.1117/12.401612
Event: International Symposium on Optical Science and Technology, 2000, San Diego, CA, United States

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.

Citation Download Citation

Marc L. Pusey and John Sumida "Fluorescence studies of protein crystal nucleation", Proc. SPIE 4098, Optical Devices and Diagnostics in Materials Science, (29 September 2000); https://doi.org/10.1117/12.401612

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