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1MUK

reovirus lambda3 native structure

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 14-BM-C
Synchrotron siteAPS
Beamline14-BM-C
Temperature [K]100
Detector technologyCCD
Collection date2002-05-01
DetectorADSC QUANTUM 4
Wavelength(s)1.000
Spacegroup nameP 21 21 21
Unit cell lengths70.874, 85.162, 248.641
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000

*

- 2.500
R-factor0.215
Rwork0.208
R-free0.24500

*

Structure solution methodMIR+MAD
RMSD bond length0.008

*

RMSD bond angle1.470

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareMLPHARE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.000

*

2.590
High resolution limit [Å]2.500

*

2.500
Rmerge0.0690.267
Total number of observations337229

*

Number of reflections52430

*

<I/σ(I)>244.7
Completeness [%]97.985
Redundancy64
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.822

*

PEG4000, sodium chloride, HEPES, glycerol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein8.7 (mg/ml)
21dropsodium HEPES50 (mM)pH7.8
31dropglycerol10 (%)
41drop150 (mM)
51dropdithiothreitol10 (mM)
61drop0.02 (%)
71reservoirPEG80007.5 (%)
81reservoirglycerol10 (%)
91reservoirsodium HEPES0.1 (M)pH7.8

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