4WNY
Crystal structure of a protein from the universal stress protein family from Burkholderia pseudomallei
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-07-02 |
Detector | RAYONIX MX-225 |
Wavelength(s) | 0.978726 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 79.260, 79.260, 39.640 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 39.630 - 2.250 |
R-factor | 0.2238 |
Rwork | 0.224 |
R-free | 0.22740 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | balbes 1mjh |
RMSD bond length | 0.002 |
RMSD bond angle | 0.489 |
Data reduction software | XDS |
Phasing software | MOLREP |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 10.060 | 2.310 |
High resolution limit [Å] | 2.250 | 7.120 | 2.250 |
Rmerge | 0.064 | 0.023 | 0.501 |
Rmeas | 0.069 | 0.025 | 0.538 |
Total number of observations | 51565 | ||
Number of reflections | 6890 | 148 | 508 |
<I/σ(I)> | 22.26 | 66.85 | 3.75 |
Completeness [%] | 97.8 | 91.9 | 100 |
Redundancy | 7.48 | 7.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 290 | Rigaku Reagents JCSG+ screen, b10: 50% PEG 200, 200mM MgCl2, 100mM Na-cacodylate pH 6.5; BupsA.17310.a.A1.PW31024 at 28.5mg/ml |