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1XJF

Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dATP complex

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsMAX II BEAMLINE I711
Synchrotron siteMAX II
BeamlineI711
Temperature [K]100
Detector technologyCCD
Collection date2002-02-17
DetectorMARRESEARCH
Wavelength(s)1.076
Spacegroup nameC 1 2 1
Unit cell lengths116.300, 123.760, 107.030
Unit cell angles90.00, 103.82, 90.00
Refinement procedure
Resolution22.880 - 2.400
R-factor0.21105
Rwork0.208
R-free0.26026
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1rlr
RMSD bond length0.016
RMSD bond angle1.651
Data scaling softwareCCP4 ((TRUNCATE))
Phasing softwareCNS
Refinement softwareREFMAC (5.1.24)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.0002.600
High resolution limit [Å]2.4002.400
Number of reflections57137
<I/σ(I)>12.13.2
Completeness [%]99.399.5
Redundancy3.75
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP4.5293PEG8000, sodium acetate, sodium chloride, dithiotreithol, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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