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 |