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2Y56

Fragment growing induces conformational changes in acetylcholine- binding protein: A structural and thermodynamic analysis - (Compound 3)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSLS BEAMLINE X06SA
Synchrotron siteSLS
BeamlineX06SA
Temperature [K]100
Detector technologyPIXEL
Collection date2010-02-05
DetectorDECTRIS PILATUS 6M
Spacegroup nameI 2 3
Unit cell lengths218.930, 218.930, 218.930
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution48.950 - 3.590
R-factor0.1752
Rwork0.174
R-free0.20250
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2c9t
RMSD bond length0.010
RMSD bond angle1.010
Data reduction softwareXDS
Data scaling softwareXSCALE
Phasing softwarePHASER
Refinement softwareBUSTER (2.8.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]16.0503.680
High resolution limit [Å]3.5903.590
Rmerge0.1400.600
Number of reflections20509
<I/σ(I)>12.312.87
Completeness [%]99.899.7
Redundancy5.415
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
18.50.1M MMT PH8.5, 1.1M AMMONIUM SULPHATE

217705

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