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1M07

RESIDUES INVOLVED IN THE CATALYSIS AND BASE SPECIFICITY OF CYTOTOXIC RIBONUCLEASE FROM BULLFROG (RANA CATESBEIANA)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X4A
Synchrotron siteNSLS
BeamlineX4A
Temperature [K]298
Detector technologyCCD
Collection date2000-08-06
DetectorADSC QUANTUM 4
Wavelength(s)1.05
Spacegroup nameP 1 21 1
Unit cell lengths28.629, 53.566, 72.203
Unit cell angles90.00, 98.31, 90.00
Refinement procedure
Resolution19.680 - 1.800
R-factor0.227
Rwork0.189
R-free0.22900

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1km8
RMSD bond length0.016
RMSD bond angle26.400

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Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]19.6801.830
High resolution limit [Å]1.800

*

1.800
Rmerge0.0730.180
Total number of observations137742

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Number of reflections20226

*

<I/σ(I)>11.16.2
Completeness [%]90.190.5
Redundancy6.812.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8

*

2980.1 M potassium sodium tartrate tetrahydrate, 24 % PEG 8000, 0.05 M sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21dropTris-HCl4 (mM)pH8.0
31drop4 (mM)
41reservoirpotassium/sodium tartrate tetrahydrate0.1 (M)
51reservoirPEG800024 (%(w/v))
61reservoirsodium citrate0.05 (M)pH5.6

239149

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