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

IUCrJ

Volumn 3, Issue , 2016, Pages 115-126

  Howard, E I ^a,b   Guillot, B ^c   Blakeley, M P ^d   Haertlein, M ^e   Moulin, M ^e   Mitschler, A ^a   Cousido Siah, A ^a   Fadel, F ^a   Valsecchi, W M ^f   Tomizaki, Takashi ^g   Petrova, T ^h   Claudot, J ^c   Podjarny, A ^a  

^a CNRS   (France)

^b UNLP ^*  (Argentina)

^c UNIVERSITÉ DE LORRAINE   (France)

^d INSTITUT LAUE LANGEVIN   (France)

^e EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

^f UNIVERSIDAD DE BUENOS AIRES   (Argentina)

^g PAUL SCHERRER INSTITUTE   (Switzerland)

^h INSTITUTE OF MATHEMATICAL PROBLEMS OF BIOLOGY   (Russian Federation)

Author keywords

AIM topological properties; fatty acid binding protein; high resolution room temperature X ray crystallography; Neutron protein crystallography; protein hydration layer

Indexed keywords

EID: 84960440601     PISSN: None     EISSN: 20522525     Source Type: Journal    
DOI: 10.1107/S2052252515024161     Document Type: Article

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