Ab Initio Semi-Quantitative Analysis of Micro-Beam Grazing-Incidence Small-Angle X-Ray Scattering (Μ-GISAXS) during Protein Crystal Nucleation and Growth

Claudio Nicolini (1, 2, 3, 4) , Nicola Luigi Bragazzi (3, 4) , Eugenia Pechkova (3, 4) , Rémi Lazzari (2)

1 ESRF - European Synchrotron Radiation Facility
2 INSP - Institut des Nanosciences de Paris
3 Department of Experimental Medicine
4 Nanoworld Institute Fondazione

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.

Domaines: Matière Condensée [cond-mat]

Claudio Nicolini, Nicola Luigi Bragazzi, Eugenia Pechkova, Rémi Lazzari. Ab Initio Semi-Quantitative Analysis of Micro-Beam Grazing-Incidence Small-Angle X-Ray Scattering (Μ-GISAXS) during Protein Crystal Nucleation and Growth. Journal of Proteomics and Bioinformatics, 2014, 07 (02), pp.064--070. ⟨10.4172/jpb.1000303⟩. ⟨hal-01243090⟩