3SLG
Crystal structure of PbgP3 protein from Burkholderia pseudomallei
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-04-23 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97740 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 83.570, 91.550, 147.260 |
Unit cell angles | 90.00, 91.63, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.100 |
R-factor | 0.1793 |
Rwork | 0.177 |
R-free | 0.22130 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1z7e |
RMSD bond length | 0.015 |
RMSD bond angle | 1.307 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER (2.1.4) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.150 | |
High resolution limit [Å] | 2.100 | 9.390 | 2.100 |
Rmerge | 0.060 | 0.013 | 0.428 |
Number of reflections | 128239 | 1483 | 9461 |
<I/σ(I)> | 14.24 | 53.95 | 2.23 |
Completeness [%] | 99.0 | 96.7 | 99.4 |
Redundancy | 2.8 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | protein at 8.2 mg/mL against PACT screen condition C10, 20% PEG 6000, 0.2 M MgCl2, 0.1 M Hepes, 20% ethylene glycol as cryo-protection reagent, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |