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2OBP

Crystal structure of a putative dna-binding protein (reut_b4095) from ralstonia eutropha jmp134 at 1.70 A resolution

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL11-1
Synchrotron siteSSRL
BeamlineBL11-1
Temperature [K]100
Detector technologyCCD
Collection date2006-12-03
DetectorMARMOSAIC 325 mm CCD
Wavelength(s)0.91837, 0.97932, 0.97910
Spacegroup nameP 63 2 2
Unit cell lengths76.580, 76.580, 137.860
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution29.412 - 1.700
R-factor0.188
Rwork0.186
R-free0.21900
Structure solution methodMAD
RMSD bond length0.016
RMSD bond angle1.511
Data reduction softwareXDS
Data scaling softwareXSCALE
Phasing softwareSHELX
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallInner shellOuter shell
Low resolution limit [Å]29.4121.760
High resolution limit [Å]1.7002.9001.700
Rmerge0.0630.0420.628
Number of reflections26996
<I/σ(I)>19.0241.33.1
Completeness [%]98.299.790.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP, NANODROP5.82770.2M MgNO3, 20.0% PEG-3350, No Buffer pH 5.8, VAPOR DIFFUSION, SITTING DROP, NANODROP, temperature 277K

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