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DENFERT version 2: extension of ab initio structural modelling of hydrated biomolecules to the case of small‐angle neutron scattering data
Author(s) -
Koutsioubas Alexandros,
Jaksch Sebastian,
Pérez Javier
Publication year - 2016
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s1600576716003393
Subject(s) - biomolecule , scattering , neutron scattering , ab initio , neutron , small angle neutron scattering , work (physics) , molecule , materials science , physics , computational physics , molecular physics , chemical physics , optics , nuclear physics , nanotechnology , thermodynamics , quantum mechanics
Following the introduction of the program DENFERT [ Koutsioubas & Pérez (2013). J. Appl. Cryst. 46 , 1884–1888], which takes into account the hydration layer around solvated biological molecules during ab initio restorations of low‐resolution molecular envelopes from small‐angle X‐ray scattering data, the present work introduces the second version of the program, which provides the ability to treat neutron scattering data sets. By considering a fully interconnected and hydrated model during the entire minimization process, it has been possible to simplify the user input and reach more objective shape reconstructions. Additionally, a new method is implemented for the subtraction of the contribution of internal inhomogeneities of biomolecules to the measured scattering. Validation of the overall approach is performed by successfully recovering the shape of various protein molecules from experimental neutron and X‐ray solution scattering data.