5DFA
3D structure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus
Replaces: 4OJYExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-10-19 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9763 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 71.730, 181.310, 197.660 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 66.806 - 2.500 |
| R-factor | 0.1605 |
| Rwork | 0.157 |
| R-free | 0.22000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kwg |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.683 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 71.700 | 2.560 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.061 | 0.198 |
| Number of reflections | 87146 | |
| <I/σ(I)> | 13.9 | |
| Completeness [%] | 97.4 | 96.6 |
| Redundancy | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 16-18% PEG 3350, 250 mM NaCl, 100 mM Hepes buffer pH 7 |
