5A55
The native structure of GH101 from Streptococcus pneumoniae TIGR4
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESAEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 76.260, 89.130, 88.570 |
Unit cell angles | 90.00, 110.91, 90.00 |
Refinement procedure
Resolution | 89.090 - 1.850 |
R-factor | 0.14439 |
Rwork | 0.143 |
R-free | 0.17879 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | NONE |
RMSD bond length | 0.012 |
RMSD bond angle | 1.467 |
Data reduction software | XDS |
Data scaling software | SCALA |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.950 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.043 | 0.380 |
Number of reflections | 88792 | |
<I/σ(I)> | 47.1 | 4.6 |
Completeness [%] | 99.1 | 98.2 |
Redundancy | 6.9 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 292 | 1:1 ratio of protein to 25% (w/v) polyethylene glycol (PEG) 1500 |