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3GP3

Crystal structure of phosphoglyceromutase from Burkholderia pseudomallei with 2-phosphoserine

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 23-ID-D
Synchrotron siteAPS
Beamline23-ID-D
Collection date2008-12-04
Wavelength(s)0.97934
Spacegroup nameP 1
Unit cell lengths49.263, 72.045, 78.036
Unit cell angles107.96, 93.00, 104.20
Refinement procedure
Resolution50.000 - 1.500
R-factor0.238
Rwork0.237
R-free0.26800
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.027
RMSD bond angle2.114
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareMOLREP
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.550
High resolution limit [Å]1.5001.500
Rmerge0.0810.598
Number of reflections149575
<I/σ(I)>18.0621.4
Completeness [%]95.384.9
Redundancy3.12.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.5289EMERALD CRYO B-4: 100MM MES PH 7.5, 5% PEG 1000, 10% GLYCEROL, 30% PEG 600, 11.7 mg/mL protein, VAPOR DIFFUSION, SITTING DROP, temperature 289K

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