4PSE
Trichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-02-04 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.93 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.043, 37.544, 133.009 |
| Unit cell angles | 90.00, 97.38, 90.00 |
Refinement procedure
| Resolution | 47.660 - 1.710 |
| R-factor | 0.2207 |
| Rwork | 0.220 |
| R-free | 0.23430 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4psc |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.150 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | BUSTER (2.11.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.780 |
| High resolution limit [Å] | 1.710 | 1.710 |
| Rmerge | 0.075 | 0.860 |
| Number of reflections | 51222 | |
| <I/σ(I)> | 10.8 | 2.15 |
| Completeness [%] | 98.0 | 95.6 |
| Redundancy | 4 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.7 | 293 | mixing 300 nl enzyme at 10 mg/ml and 30 mM betaOG with 100 nl of PEG3350 (17%), BIS-TRIS (0.1 M), pH 5.7, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
