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1FO1

CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE MRNA EXPORT FACTOR TAP

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsELETTRA BEAMLINE 5.2R
Synchrotron siteELETTRA
Beamline5.2R
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1999-10-14
DetectorMARRESEARCH
Spacegroup nameP 43 21 2
Unit cell lengths96.354, 96.354, 152.227
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000 - 2.900
R-factor0.25
Rwork0.250
R-free0.27800
RMSD bond length0.007
RMSD bond angle1.260
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0003.000
High resolution limit [Å]2.9002.900
Rmerge0.0570.235
Total number of observations67191

*

Number of reflections16300
<I/σ(I)>21
Completeness [%]98.593
Redundancy4.1

*

4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

6.84

*

PEG 8000, EDTA, cacodylate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein20 (mg/ml)
21reservoircacodylate100 (mM)
31reservoirPEG800018 (%(w/v))
41reservoirEDTA20 (mM)

246031

PDB entries from 2025-12-10

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