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1MT3

Crystal Structure of the Tricorn Interacting Factor Selenomethionine-F1

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsMPG/DESY, HAMBURG BEAMLINE BW6
Synchrotron siteMPG/DESY, HAMBURG
BeamlineBW6
Temperature [K]100
Detector technologyCCD
Collection date2001-09-04
DetectorMARRESEARCH
Wavelength(s)0.9788, 0.9795, 0.9500
Spacegroup nameP 21 21 21
Unit cell lengths51.968, 60.759, 80.678
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 2.000
R-factor0.285
Rwork0.255
R-free0.28000
Structure solution methodMAD
RMSD bond length0.012
RMSD bond angle1.594
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHARP
Refinement softwareCNS
Data quality characteristics
 Overall
Low resolution limit [Å]20.000
High resolution limit [Å]2.000
Rmerge0.064
Number of reflections33131

*

<I/σ(I)>24.6
Completeness [%]99.0

*

Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

629312% PEG 6000, 100 mM MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein20 (mg/ml)
21reservoirMES100 (mM)pH6.0
31reservoirBis-Tris-HCl100 (mM)pH6.0
41reservoirPEG60007-12 (%)
51reservoirHEPES100 (mM)pH7.5
61reservoirPEG800020 (%)

219869

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