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 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.
Pechkova
E
E
Nanoworld Institute, CIRSDNNOB-University of Genova and Fondazione Elba, Rome, Italy.
Tripathi
S
S
Spera
R
R
Nicolini
C
C
D018834:Chaperonin 60 / Q000737:chemistry*; D003460:Crystallization / Q000379:methods*; D004926:Escherichia coli; D049329:Nanostructures / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
D018834:Chaperonin 60