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2O29

Spectroscopic and Structural Study of the Heterotropic Linkage between Halide and Proton Ion Binding to Gfp Proteins: E2(GFP)-BR Complex

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM30A
Synchrotron siteESRF
BeamlineBM30A
Temperature [K]100
Detector technologyCCD
Spacegroup nameP 21 21 21
Unit cell lengths51.144, 62.852, 69.172
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution15.150 - 1.800
R-factor0.17909
Rwork0.178
R-free0.20835
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2h6v
RMSD bond length0.011
RMSD bond angle1.523
Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Phasing softwareMOLREP
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.6841.900
High resolution limit [Å]1.8001.800
Rmerge0.0980.377
Number of reflections20873
<I/σ(I)>6.92
Completeness [%]97.795.2
Redundancy5.26.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP514% (W/V) PEG 3350, 100 MM NH4 ACETATE, 0.2 M NH4Br, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 100K

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PDB entries from 2024-05-15

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