5KET
Structure of the aldo-keto reductase from Coptotermes gestroi
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LNLS BEAMLINE W01B-MX2 |
| Synchrotron site | LNLS |
| Beamline | W01B-MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-03-24 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 1.46 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 131.141, 131.141, 290.657 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.744 - 2.850 |
| R-factor | 0.2417 |
| Rwork | 0.239 |
| R-free | 0.29300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hbk |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.968 |
| Data scaling software | Aimless (0.5.8) |
| Phasing software | PHASER (2.5.7) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 44.740 | 44.740 | 3.000 |
| High resolution limit [Å] | 2.850 | 9.010 | 2.850 |
| Rmerge | 0.290 | 0.046 | 1.648 |
| Rmeas | 0.309 | 0.049 | 1.772 |
| Rpim | 0.105 | 0.017 | 0.643 |
| Total number of observations | 195360 | 6127 | 24398 |
| Number of reflections | 22740 | ||
| <I/σ(I)> | 8.6 | 33 | 1.5 |
| Completeness [%] | 99.8 | 97.6 | 99.9 |
| Redundancy | 8.6 | 8 | 7.5 |
| CC(1/2) | 0.987 | 0.999 | 0.536 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 0.1 M magnesium sulfate, 10% PEG400, 2 M ammonium phosphate dibasic |
