3C9X
Crystal structure of Trichoderma reesei aspartic proteinase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LNLS BEAMLINE D03B-MX1 |
| Synchrotron site | LNLS |
| Beamline | D03B-MX1 |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2006-01-01 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.50 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 74.171, 74.171, 161.530 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.460 - 1.700 |
| R-factor | 0.182 |
| Rwork | 0.179 |
| R-free | 0.21290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bxo |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.681 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.460 | 1.790 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.076 | 0.073 |
| Number of reflections | 50475 | |
| <I/σ(I)> | 8.3 | 2 |
| Completeness [%] | 98.4 | 98.8 |
| Redundancy | 3.9 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | 15% PEG3350, 50mM potassium buffer, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
