Groel crystal growth and characterization

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 i...

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Bibliographic Details
Published in:BioSystems 2008-12, Vol.94 (3), p.223-227
Main Authors: Pechkova, E., Tripathi, S., Spera, R., Nicolini, C.
Format: Article
Language:English
Subjects:
Chaperonin 60 - chemistry
Crystallization
Crystallization - methods
Escherichia coli
GroEL
LB protein thin film
Nanostructures - chemistry
Ribosomal proteins
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Structure-Activity Relationship
X-Ray Diffraction
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Summary: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.
ISSN:0303-2647
1872-8324
DOI:10.1016/j.biosystems.2008.05.031