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1AFU

STRUCTURE OF RIBONUCLEASE A AT 2.0 ANGSTROMS FROM MONOCLINIC CRYSTALS

Experimental procedure
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.6
Synchrotron siteSRS
BeamlinePX9.6
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1995-07
DetectorMARRESEARCH
Spacegroup nameC 1 2 1
Unit cell lengths101.840, 33.430, 73.670
Unit cell angles90.00, 90.02, 90.00
Refinement procedure
Resolution8.000 - 2.000
R-factor0.201
Rwork0.201
R-free0.28500
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)3rn3
RMSD bond length0.012
RMSD bond angle25.300

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.100
High resolution limit [Å]2.0002.000
Rmerge0.044

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Total number of observations38250

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Number of reflections15331
<I/σ(I)>18.110.4
Completeness [%]89.679.5
Redundancy2.51.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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5.516

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PROTEIN WAS CRYSTALLIZED FROM 20 MM SODIUM CITRATE BUFFER PH 5.5 AND 20 % PEG 4000.
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21dropsodium citrate10 (mM)
31dropPEG400010 (%)
41reservoirPEG400020 (%)
51reservoirsodium citrate20 (M)

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