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1I3F

Ribonuclease T1 V89S mutant

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineX11
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1999-08-14
DetectorMARRESEARCH
Wavelength(s)0.909
Spacegroup nameP 21 21 21
Unit cell lengths40.308, 46.886, 49.901
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000

*

- 2.350
R-factor0.173

*

Rwork0.173
R-free0.28340
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.008
RMSD bond angle1.493
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.430
High resolution limit [Å]2.3502.350
Rmerge0.1510.406
Total number of observations13465

*

Number of reflections4178
<I/σ(I)>7.113.13
Completeness [%]98.697.7
Redundancy3.223.25
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP4.2293Zegers, I., (1998) Nat.Struct.Biol., 5, 280.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropRNase T115 (mg/ml)
21dropexo-cGPS15 (mM)
31drop20 (mM)
41drop2 (mM)
51reservoirMPD55 (%(v/v))

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PDB entries from 2024-05-15

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