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4KEX

Crystal structure analysis of a single amino acid deletion mutation in EGFP

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsDIAMOND BEAMLINE I04
Synchrotron siteDiamond
BeamlineI04
Wavelength(s)0.97630
Spacegroup nameP 21 21 21
Unit cell lengths51.450, 63.140, 65.700
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution45.570 - 1.600
R-factor0.1837
Rwork0.182
R-free0.20920
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)4eul
RMSD bond length0.023
RMSD bond angle2.139
Data scaling softwareSCALA (0.1.16)
Phasing softwarePHASER (2.5.1)
Refinement softwareREFMAC (5.7.0029)
Data quality characteristics
 Overall
Low resolution limit [Å]51.450
High resolution limit [Å]1.600
Rmerge0.092
Number of reflections28209
<I/σ(I)>15.2
Completeness [%]98.1
Redundancy7.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION42910.1 M MMT Buffer (Malic acid, MES and Tris), 25% (w/v) PEG 1500, pH 4.0, VAPOR DIFFUSION, temperature 291K

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