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3IGR

The Crystal Structure of Ribosomal-protein-S5-alanine Acetyltransferase from Vibrio fischeri to 2.0A

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-ID
Synchrotron siteAPS
Beamline19-ID
Temperature [K]100
Detector technologyCCD
Collection date2009-06-19
DetectorADSC QUANTUM 315
Wavelength(s)0.9794
Spacegroup nameC 2 2 21
Unit cell lengths63.504, 107.173, 145.719
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution50.000 - 2.000
R-factor0.207
Rwork0.205
R-free0.23700
RMSD bond length0.012
RMSD bond angle1.278
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Refinement softwareREFMAC (refmac_5.5.0102)
Data quality characteristics
 OverallInner shellOuter shell
Low resolution limit [Å]50.00050.0002.070
High resolution limit [Å]2.0004.3102.000
Rmerge0.0940.0560.700
Number of reflections34070
<I/σ(I)>6.4
Completeness [%]99.898.9100
Redundancy4.94.84.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP927710% PEG 20000, 2% Dioxane, 0.1M Bicine pH 9, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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