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1I9S

CRYSTAL STRUCTURE OF THE RNA TRIPHOSPHATASE DOMAIN OF MOUSE MRNA CAPPING ENZYME

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL9-1
Synchrotron siteSSRL
BeamlineBL9-1
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2000-04-15
DetectorMARRESEARCH
Wavelength(s)0.97
Spacegroup nameC 2 2 21
Unit cell lengths62.228, 98.856, 71.818
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution27.000 - 1.650
R-factor0.196
Rwork0.194
R-free0.22500
Structure solution methodMAD
RMSD bond length0.010

*

RMSD bond angle1.600

*

Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Phasing softwareMLPHARE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]27.0001.690
High resolution limit [Å]1.6501.650
Rmerge0.0930.282
Total number of observations143292

*

Number of reflections26506
<I/σ(I)>5.22.9
Completeness [%]99.498.6
Redundancy5.44.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.510

*

15% isopropanol, 50mM sodium cacodylate (pH 6.5), 25mM magnesium chloride, 25mM ammonium sulfate , VAPOR DIFFUSION, HANGING DROP, temperature 283K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein5 (mg/ml)
21reservoirisopropanol15 (%)
31reservoirsodium cacodylate50 (mM)
41reservoir25 (mM)
51reservoirammonium sulfate25 (mM)

220113

PDB entries from 2024-05-22

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