4PSC
Structure of cutinase from Trichoderma reesei in its native form.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-01-01 |
| Detector | PSI PILATUS 6M |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 29.159, 48.002, 141.579 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 79.320 - 1.150 |
| R-factor | 0.147 |
| Rwork | 0.146 |
| R-free | 0.16700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cex |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.951 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 79.320 | |
| High resolution limit [Å] | 1.150 | |
| Rmerge | 0.075 | |
| Number of reflections | 81001 | |
| <I/σ(I)> | 12.3 | |
| Completeness [%] | 91.0 | |
| Redundancy | 3.9 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 293 | mixing 300 nl enzyme at 10 mg/ml with 100 nl of PEG3350 (25%), Sodium Chloride (0.2 M), BIS-TRIS (0.1 M), pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
