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1DT9

THE CRYSTAL STRUCTURE OF HUMAN EUKARYOTIC RELEASE FACTOR ERF1-MECHANISM OF STOP CODON RECOGNITION AND PEPTIDYL-TRNA HYDROLYSIS

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7A
Detector technologyCCD
Spacegroup nameP 43 21 2
Unit cell lengths77.080, 77.080, 194.440
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 2.700
Rwork0.246
R-free0.31400
RMSD bond length0.014
RMSD bond angle2.000
Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Phasing softwareSHARP
Refinement softwareCNS (0.9)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.00025.000
High resolution limit [Å]2.7002.700
Rmerge0.0500.406
Total number of observations82505

*

Number of reflections16712

*

<I/σ(I)>8.3
Completeness [%]99.298
Redundancy4.93.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.520

*

protein was mixed with equal volume of reservoir solution

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21reservoirHEPES100 (mM)
31reservoirPEG400014-22 (%(w/v))
41reservoirglycerol15 (%(v/v))
51reservoir200 (mM)

227561

PDB entries from 2024-11-20

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