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1MXR

High resolution structure of Ribonucleotide reductase R2 from E. coli in its oxidised (Met) form

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM1A
Synchrotron siteESRF
BeamlineBM1A
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1999-02-08
DetectorMARRESEARCH
Wavelength(s)0.87961
Spacegroup nameP 21 21 21
Unit cell lengths73.844, 84.975, 114.318
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution40.000

*

- 1.420
R-factor0.16
Rwork0.160
R-free0.18500
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)reduced e. coli RNR R2 (1XIK)
RMSD bond length0.013
RMSD bond angle1.510

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]40.0001.470
High resolution limit [Å]1.4201.420
Rmerge0.064

*

0.288
Total number of observations603231

*

Number of reflections123371
Completeness [%]90.891.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP620

*

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

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG400020 (%)
21reservoir0.2 (M)
31reservoirdioxane3 (%)
41reservoirMES0.05 (M)
51reservoirEMTS

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PDB entries from 2024-07-17

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