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4EN1

The 1.62A structure of a FRET-optimized Cerulean Fluorescent Protein

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 8.2.1
Synchrotron siteALS
Beamline8.2.1
Temperature [K]100
Detector technologyCCD
Collection date2011-01-30
DetectorADSC QUANTUM 315
Spacegroup nameP 21 21 21
Unit cell lengths79.410, 88.726, 94.738
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution29.980 - 1.620
R-factor0.179
Rwork0.178
R-free0.20500
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2wso
RMSD bond length0.018
RMSD bond angle2.380
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwarePHASER
Refinement softwareREFMAC (5.6.0117)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.650
High resolution limit [Å]1.6201.620
Rmerge0.0710.477
Number of reflections79895
<I/σ(I)>14.52.04
Completeness [%]94.599
Redundancy33
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
14.7298mother liquor consisting of 0.08 M sodium acetate trihydrate, 0.16 M ammonium sulfate, 9% (w/v) PEG4000, and 19% (v/v) glycerol. Hanging drops contained 2 uL protein solution and 1 uL mother liquor, pH 4.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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