Ab Initio Semi-Quantitative Analysis of Micro-Beam Grazing-Incidence Small-Angle X-Ray Scattering (ÃÂ-GISAXS) during Protein Crystal Nucleation and Growth
- *Corresponding Author:
- Claudio Nicolini
Biophysics and Nanobiotechnology Laboratories (BNL)
Department of Experimental Medicine (DIMES), University of Genoa
Via Antonio Pastore 3, Genoa 16132, Italy
Tel: +39 010 353 38217
E-mail: [email protected]
Received Date: November 01, 2013; Accepted Date: February 18, 2014; Published Date: February 21, 2014
Citation: Nicolini C, Bragazzi NL, Pechkova E, Lazzari R (2014) Ab Initio Semi- Quantitative Analysis of Micro-Beam Grazing-Incidence Small-Angle X-Ray Scattering (M-GISAXS) during Protein Crystal Nucleation and Growth. J Proteomics Bioinform 7:064-070. doi: 10.4172/jpb.1000303
Copyright: © 2014 Nicolini C, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Micro-beam Grazing-Incidence Small-Angle X-ray scattering (μ-GISAXS), exploiting both the advantages of elastic X-ray scattering and the highly focused third-generation synchrotron radiation micro-beams, is an advanced scattering technique that enables scientists to unravel the details of crystal growth processes and to investigate large-scale structures in thin films, including nanobiofilms or other different kinds of surfaces, such as surface gradients or confined surfaces. In this study, we analyze semi-quantitatively and we simulate our previously acquired μ-GISAXS experiments of Thaumatin and Lysozyme Langmuir-Blodgett (LB)-film, shedding light on nucleation and crystal growth processes. Here, we show that, during LB-thin film facilitated nucleation, the particle radius of Thaumatin and of Lysozyme crystal increases while the film thickness reduces. Structural re-organization inside and within the LB-thin film are likely to lead to the crystal nucleation and growth. These semi-quantitative findings are in agreement with the model previously hypothesized. New insights and implications for protein nanocrystallography are also discussed.