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5UUO

Crystal structure of SARO_2595 from Novosphingobium aromaticivorans

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 23-ID-B
Synchrotron siteAPS
Beamline23-ID-B
Temperature [K]100
Detector technologyPIXEL
Collection date2016-06-30
DetectorDECTRIS EIGER X 16M
Wavelength(s)0.7749
Spacegroup nameP 21 21 21
Unit cell lengths68.810, 70.390, 168.230
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution29.810 - 1.250
R-factor0.1303
Rwork0.130
R-free0.13230
RMSD bond length0.007
RMSD bond angle1.024
Data reduction softwareXSCALE (May 1, 2016 BUILT=20160617)
Data scaling softwareXDS (VERSION Oct 15, 2015)
Phasing softwarePHASER (2.6.0)
Refinement softwarePHENIX ((1.11.1_2575: ???))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]29.3601.280
High resolution limit [Å]1.2501.250
Rmerge0.0521.297
Rpim0.0150.356
Number of reflections22544216479
<I/σ(I)>21.851.96
Completeness [%]99.999.8
Redundancy13.513.9
CC(1/2)1.0000.841
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.5293Saro protein at 277 mM was incubated with 10 mM reduced glutathione for 50 minutes prior to setting up crystallization experiments. The droplet yielding the crystal with the highest observed diffracting power was composed of 130 nL protein and 85 nL reservoir solution. The reservoir solution was 1.35 M ammonium sulfate, 0.1 M lithium sulfate 0.1 M bis-trispropane, pH 7.5

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