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1XSM

PROTEIN R2 OF RIBONUCLEOTIDE REDUCTASE FROM MOUSE

Experimental procedure
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.6
Synchrotron siteSRS
BeamlinePX9.6
Temperature [K]277
Detector technologyIMAGE PLATE
Collection date1992-02-15
DetectorRIGAKU RAXIS IIC
Spacegroup nameC 2 2 21
Unit cell lengths77.078, 108.932, 92.900
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution25.000 - 2.300
R-factor0.191
Rwork0.191
R-free0.25000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1rib
RMSD bond length0.018
RMSD bond angle28.600

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.0002.380
High resolution limit [Å]2.3002.290
Rmerge0.1040.300

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Total number of observations144719

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Number of reflections17131
<I/σ(I)>17.6
Completeness [%]95.8

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70.9
Redundancy8.84
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

4.720

*

Nielsen, B.B., (1995) FEBS Letters, 373, 310.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein7.5 (mg/ml)
21drop0.8-1.0 (M)
31dropacetate50 (mM)
41reservoir0.8-1.0 (M)
51reservoiracetate50 (mM)

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PDB entries from 2024-05-15

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