3FV3
Secreted aspartic protease 1 from Candida parapsilosis in complex with pepstatin A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-07-10 |
| Detector | SBC-3 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 86.488, 194.247, 97.147 |
| Unit cell angles | 90.00, 91.52, 90.00 |
Refinement procedure
| Resolution | 46.030 - 1.850 |
| R-factor | 0.16646 |
| Rwork | 0.166 |
| R-free | 0.19014 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1eag |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.256 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.3.0037) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.900 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.045 | 0.490 |
| Number of reflections | 273011 | |
| <I/σ(I)> | 27.2 | 2.4 |
| Completeness [%] | 99.3 | 98.5 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 292 | five-fold molar inhibitor excess, Cpr=8mg/ml; drops: 0.002ml protein + 0.001ml reservoir + 0.0002ml 10mM ZnAc; reservoir: 0.1M Tris pH 7.0, 2.0M Ammonium Sulfate, 10% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
