High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP–oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution

High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP–oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution

Crystal diffraction data of heart fatty acid binding protein (H-FABP) in complex with oleic acid were measured at room temperature with high-resolution X-ray and neutron protein crystallography (0.98 and 1.90 Å resolution, respectively). These data provided very detailed information about the cluste...

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Bibliographic Details
Main Authors: E. I. Howard, B. Guillot, M. P. Blakeley, M. Haertlein, M. Moulin, A. Mitschler, A. Cousido-Siah, F. Fadel, W. M. Valsecchi, Takashi Tomizaki, T. Petrova, J. Claudot, A. Podjarny
Format: Article
Language:English
Published: International Union of Crystallography 2016-03-01
Series:IUCrJ
Subjects:
Neutron protein crystallography
high-resolution room-temperature X-ray crystallography
fatty acid binding protein
protein hydration layer
AIM topological properties
Online Access:http://scripts.iucr.org/cgi-bin/paper?S2052252515024161

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http://scripts.iucr.org/cgi-bin/paper?S2052252515024161

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