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1I4W

THE CRYSTAL STRUCTURE OF THE TRANSCRIPTION FACTOR SC-MTTFB OFFERS INTRIGUING INSIGHTS INTO MITOCHONDRIAL TRANSCRIPTION

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-ID
Synchrotron siteAPS
Beamline19-ID
Temperature [K]100
Detector technologyCCD
Collection date1999-11-21
DetectorMARRESEARCH
Wavelength(s)1.0
Spacegroup nameC 1 2 1
Unit cell lengths90.418, 44.684, 99.819
Unit cell angles90.00, 110.23, 90.00
Refinement procedure
Resolution19.880 - 2.600
R-factor0.187
Rwork0.187
R-free0.27400
Structure solution methodSIRAS
RMSD bond length0.007
RMSD bond angle1.400
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareISIR
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.700
High resolution limit [Å]2.6002.600
Rmerge0.060

*

0.170
Total number of observations202625

*

Number of reflections10896
<I/σ(I)>19.54.6
Completeness [%]90.863.4
Redundancy53.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8

*

291Schubot, G.S., (2000) Acta Crystallogr., D56, 902.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21reservoir300 (mM)
31reservoirglycerol10 (%)
41reservoirTris-HCl50 (mM)

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