3T9W
Small laccase from Amycolatopsis sp. ATCC 39116
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-10 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.97857 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 110.180, 110.180, 178.820 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.657 - 1.500 |
| R-factor | 0.1736 |
| Rwork | 0.172 |
| R-free | 0.20150 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3cg8 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.389 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (dev_764) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 20.000 | 20.000 | 1.540 |
| High resolution limit [Å] | 1.500 | 6.710 | 1.500 |
| Rmerge | 0.065 | 0.043 | 0.810 |
| Number of reflections | 66783 | 782 | 4905 |
| <I/σ(I)> | 18.46 | 44.58 | 2.6 |
| Completeness [%] | 99.9 | 94.7 | 100 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | Protein concentration was 20 mg/mL buffered with 20 mM Tris (pH 7.9), the precipitant contained 3.0 M NaCl and 100 mM Hepes, VAPOR DIFFUSION, HANGING DROP, temperature 277K |






