3GP3
Crystal structure of phosphoglyceromutase from Burkholderia pseudomallei with 2-phosphoserine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Collection date | 2008-12-04 |
Wavelength(s) | 0.97934 |
Spacegroup name | P 1 |
Unit cell lengths | 49.263, 72.045, 78.036 |
Unit cell angles | 107.96, 93.00, 104.20 |
Refinement procedure
Resolution | 50.000 - 1.500 |
R-factor | 0.238 |
Rwork | 0.237 |
R-free | 0.26800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.027 |
RMSD bond angle | 2.114 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.081 | 0.598 |
Number of reflections | 149575 | |
<I/σ(I)> | 18.062 | 1.4 |
Completeness [%] | 95.3 | 84.9 |
Redundancy | 3.1 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | EMERALD 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 |