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4C3T

The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsDIAMOND BEAMLINE I03
Synchrotron siteDiamond
BeamlineI03
Temperature [K]100
Spacegroup nameP 43 21 2
Unit cell lengths80.930, 80.930, 154.620
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution57.230 - 1.690
R-factor0.22284
Rwork0.221
R-free0.25175
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1kop
RMSD bond length0.007
RMSD bond angle1.241
Phasing softwareMOLREP
Refinement softwareREFMAC (5.7.0032)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]80.9301.740
High resolution limit [Å]1.6901.690
Rmerge0.0701.230
Number of reflections734424
<I/σ(I)>18.62.3
Completeness [%]100.0100
Redundancy12.712.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
10.5 M LICL, 50 MM SODIUM CITRATE, 10% PEG6000, PH 4.0

220113

PDB entries from 2024-05-22

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