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1OMS

Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron siteEMBL/DESY, Hamburg
BeamlineBW7A
Temperature [K]100
Detector technologyCCD
Collection date2002-11-28
DetectorMARRESEARCH
Wavelength(s)0.9797, 0.9404
Spacegroup nameH 3 2
Unit cell lengths71.644, 71.644, 375.409
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution29.900 - 2.300
R-factor0.208
Rwork0.208
R-free0.23800
Structure solution methodMAD
RMSD bond length0.008
RMSD bond angle22.900

*

Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Phasing softwareSHARP
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.420
High resolution limit [Å]2.3002.300
Rmerge0.0590.330
Number of reflections31810

*

<I/σ(I)>33.36.6
Completeness [%]99.6100
Redundancy4.2

*

4.1

*

Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP4.66

*

PEG 2000 MME, PEG 400, ammonium sulfate, sodium acetate, tris, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 279K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein1.5 (mg/ml)
21reservoirPEG2000 MME30 (%)
31reservoirsodium acetate85 (mM)
41reservoirTris-base100 (mM)
51reservoirglycerol15 (%)

227111

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