Structural characterization of gephyrin by AFM and SAXS reveals a mixture of compact and extended states

Acta Crystallographica Section D: Biological Crystallography

Volumn 69, Issue 10, 2013, Pages 2050-2060

  Sander, Bodo ^a   Tria, Giancarlo ^b,c   Shkumatov, Alexander V ^b   Kim, Eun Young ^d   Grossmann, J Günter ^e   Tessmer, Ingrid ^a   Svergun, Dmitri I ^b   Schindelin, Hermann ^a  

^a UNIVERSITY OF WÜRZBURG   (Germany)

^b DESY   (Germany)

^c UNIVERSITY OF HAMBURG   (Germany)

^d STONY BROOK UNIVERSITY   (United States)

^e UNIVERSITY OF LIVERPOOL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID A RECEPTOR; CARRIER PROTEIN; ESCHERICHIA COLI PROTEIN; GEPHYRIN; GLYCINE RECEPTOR; MEMBRANE PROTEIN; METALLOPROTEIN; MOG PROTEIN, E COLI; MOLYBDENUM COFACTOR; PTERIDINE DERIVATIVE;

ANIMAL; ARTICLE; ATOMIC FORCE MICROSCOPY; BIOSYNTHESIS; CHEMISTRY; CIRCULAR DICHROISM; COENZYME; ENSEMBLE-OPTIMIZATION METHOD; GABAA RECEPTOR; GENETIC VARIABILITY; GENETICS; INTRINSIC DISORDER; METHODOLOGY; MOCO BIOSYNTHESIS; MOLECULAR DYNAMICS; NERVE CELL INHIBITION; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; RAT; RECEPTOR CLUSTERING; SINGLE-MOLECULE ANALYSIS; SMALL ANGLE SCATTERING; SMALL-ANGLE X-RAY SCATTERING; ULTRASTRUCTURE; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

ATOMIC FORCE MICROSCOPY; ENSEMBLE-OPTIMIZATION METHOD; GABAA RECEPTOR; GEPHYRIN; GLYCINE RECEPTOR; INTRINSIC DISORDER; MOCO BIOSYNTHESIS; RECEPTOR CLUSTERING; SINGLE-MOLECULE ANALYSIS; SMALL-ANGLE X-RAY SCATTERING;

ANIMALS; CARRIER PROTEINS; CIRCULAR DICHROISM; COENZYMES; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI PROTEINS; GENETIC VARIATION; MEMBRANE PROTEINS; METALLOPROTEINS; MICROSCOPY, ATOMIC FORCE; MOLECULAR DYNAMICS SIMULATION; NEURAL INHIBITION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEOLYSIS; PTERIDINES; RATS; RECEPTORS, GABA-A; RECEPTORS, GLYCINE; SCATTERING, SMALL ANGLE; X-RAY DIFFRACTION;

EID: 84885462782     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444913018714     Document Type: Article

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