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1RSR

azide complex of the diferrous F208A mutant R2 subunit of ribonucleotide reductase

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM1A
Synchrotron siteESRF
BeamlineBM1A
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1992-09-22
DetectorMARRESEARCH
Wavelength(s)1.00
Spacegroup nameP 21 21 21
Unit cell lengths73.800, 84.200, 113.500
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution25.000 - 2.000
R-factor0.197

*

Rwork0.197
R-free0.28900
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.020
RMSD bond angle1.600
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareTNT
Refinement softwareTNT
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.0002.030
High resolution limit [Å]2.0002.000
Rmerge0.063

*

Total number of observations144767

*

Number of reflections43085
Completeness [%]88.771.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP620

*

Nordlund, P., (1989) FEBS Lett., 258, 251.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein20 (mg/ml)
21reservoirPEG400020 (%)
31reservoir0.2 (M)
41reservoirdioxane0.3 (%)
51reservoirMES0.05 (M)pH6.0

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