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6C62

An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron siteAustralian Synchrotron
BeamlineMX2
Temperature [K]100
Detector technologyPIXEL
Collection date2017-07-15
DetectorDECTRIS EIGER X 16M
Wavelength(s)0.99989
Spacegroup nameI 1 2 1
Unit cell lengths79.489, 89.040, 141.672
Unit cell angles90.00, 101.89, 90.00
Refinement procedure
Resolution69.300 - 1.950
R-factor0.15478
Rwork0.153
R-free0.19066
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)3ip4 and 3dha
RMSD bond length0.017
RMSD bond angle1.726
Data reduction softwareDIALS
Data scaling softwareAimless
Phasing softwareMoRDa
Refinement softwareREFMAC (5.8.0189)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]69.3001.990
High resolution limit [Å]1.9501.950
Rmerge0.2331.545
Rpim0.0950.622
Number of reflections704264504
<I/σ(I)>6.9
Completeness [%]100.0100
Redundancy6.97.1
CC(1/2)0.9910.804
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP6281100mM bis-tris at pH 6.0, 276 mM MgCl2, 17.6 (w/v) PEG 8000 in the reservoir with protein at 1.1 mg/mL with 0.05% agarose gel in 250 plus 250 nL drops at 8 C.

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