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7OAF

conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A, crystal form III

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSLS BEAMLINE X10SA
Synchrotron siteSLS
BeamlineX10SA
Temperature [K]100
Detector technologyPIXEL
Collection date2020-06-15
DetectorDECTRIS EIGER2 X 16M
Wavelength(s)0.9998
Spacegroup nameP 1 21 1
Unit cell lengths26.010, 38.849, 128.811
Unit cell angles90.00, 96.18, 90.00
Refinement procedure
Resolution33.214 - 1.450
Rwork0.198
R-free0.21500
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)7oaa
RMSD bond length0.018
RMSD bond angle1.654
Data reduction softwareXDS
Data scaling softwareXDS
Phasing softwareMOLREP
Refinement softwareREFMAC (5.8.0049 2013/06/30)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]33.2141.540
High resolution limit [Å]1.4501.450
Rmerge0.0830.835
Number of reflections455927257
<I/σ(I)>11.321.77
Completeness [%]99.899.4
Redundancy6.626.3
CC(1/2)1.0000.960
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP2940.1M tri-sodium citrate pH 4.5, 9.3% PEG 6000

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