Groel crystal growth and characterization

Bio Systems
Eugenia PechkovaClaudio Nicolini

Abstract

Single crystals of ribosomal proteins obtained for the first time by Langmuir-Blodgett (LB) nanotemplate confirm earlier findings (Pechkova et al., 2008), pointing to a new generation of bionanomaterials of unique structure-function relationship. The ribosomal protein phage GroEL was overexpressed in E. coli. Since these protein's samples have some difficulties by classical vapour diffusion method to yield optimal diffraction quality and order (GroEL), the LB nanotemplate method has been applied and compared to the classical method. With the thin film nanotemplate method large phage GroEL crystals appeared in few days and were subsequently characterized by MALDI-TOF Mass Spectroscopy and by a very preliminary X-ray diffraction.

References

Mar 29, 1993·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·A L Horwich, K R Willison
Dec 24, 1996·Proceedings of the National Academy of Sciences of the United States of America·R ZahnA R Fersht
Dec 4, 2003·Acta Crystallographica. Section D, Biological Crystallography·Eugenia PechkovaClaudio Nicolini
Mar 24, 2004·Trends in Biotechnology·Eugenia Pechkova, Claudio Nicolini
Sep 20, 2005·Current Opinion in Structural Biology·Christian RiekelGebhard Schertler

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Citations

Dec 1, 2017·Nature Protocols·Eugenia Pechkova, Claudio Nicolini

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