6ETZ
Cold-adapted beta-D-galactosidase from Arthrobacter sp. 32cB
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-09-24 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.987 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 137.784, 137.784, 127.208 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 46.730 - 1.800 |
| R-factor | 0.1618 |
| Rwork | 0.161 |
| R-free | 0.19750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yq2 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.874 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 46.730 | 46.730 | 1.910 |
| High resolution limit [Å] | 1.800 | 5.360 | 1.800 |
| Rmerge | 0.107 | 0.037 | 1.288 |
| Rmeas | 0.113 | 0.039 | 1.361 |
| Total number of observations | 1287351 | ||
| Number of reflections | 128996 | 5133 | 20271 |
| <I/σ(I)> | 14.46 | 48.57 | 1.51 |
| Completeness [%] | 99.5 | 99.7 | 97.5 |
| Redundancy | 9.98 | 9.423 | 9.59 |
| CC(1/2) | 0.999 | 0.999 | 0.814 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | 35% Tacsimate pH 8.0 |






