6QUC
Truncated beta-galactosidase III from Bifidobacterium bifidum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2012-05-14 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 118.500, 119.683, 144.602 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.100 - 2.300 |
R-factor | 0.1884 |
Rwork | 0.188 |
R-free | 0.21760 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3gm8 |
RMSD bond length | 0.003 |
RMSD bond angle | 0.651 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX ((1.14_3260: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.100 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.040 | 0.382 |
Number of reflections | 91305 | 9057 |
<I/σ(I)> | 8.5 | 1.7 |
Completeness [%] | 99.0 | 99 |
Redundancy | 2 | 2 |
CC(1/2) | 0.995 | 0.854 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 277 | 25% PEG 550mme 100 mM Imidazole |