6F5K
Crystal structure of laccase from Myceliophthora thermophila
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-04-06 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.966 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 67.449, 128.426, 163.624 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.230 - 1.620 |
| R-factor | 0.1521 |
| Rwork | 0.150 |
| R-free | 0.18860 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2q9o |
| RMSD bond length | 0.021 |
| RMSD bond angle | 2.085 |
| Data reduction software | XDS |
| Data scaling software | SCALA (0.5.24) |
| Phasing software | MOLREP |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 48.230 | 48.230 | 1.680 |
| High resolution limit [Å] | 1.620 | 6.270 | 1.620 |
| Rmerge | 0.109 | 0.054 | 0.866 |
| Rmeas | 0.123 | 0.061 | 0.971 |
| Rpim | 0.055 | 0.028 | 0.431 |
| Number of reflections | 89938 | 1703 | 8718 |
| <I/σ(I)> | 7.6 | 19.3 | 1.6 |
| Completeness [%] | 99.6 | 99.3 | 99.6 |
| Redundancy | 4.9 | 4.7 | 5 |
| CC(1/2) | 0.995 | 0.994 | 0.688 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 3 ul protein (66 mg/ml) + 2 ul reservoir solution (0.1 M HEPES pH 7.5, 34 % PEG 400, 0.22 M CaCl2, 0.05 M glycine) |
