2YGL
The X-ray crystal structure of tandem CBM51 modules of Sp3GH98, the family 98 glycoside hydrolase from Streptococcus pneumoniae SP3-BS71
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 | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 76.040, 90.580, 119.850 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.910 - 2.100 |
R-factor | 0.21142 |
Rwork | 0.210 |
R-free | 0.24671 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vnr |
RMSD bond length | 0.006 |
RMSD bond angle | 0.931 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.210 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.100 | 0.380 |
Number of reflections | 46386 | |
<I/σ(I)> | 22.9 | 7.3 |
Completeness [%] | 99.7 | 99.7 |
Redundancy | 13.6 | 13.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 |