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 |