1YBW
Protease domain of HGFA with no inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-12-21 |
| Detector | CUSTOM-MADE |
| Wavelength(s) | 0.917 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.430, 76.430, 72.150 |
| Unit cell angles | 90.00, 107.77, 90.00 |
Refinement procedure
| Resolution | 47.940 - 2.700 |
| R-factor | 0.218 |
| Rwork | 0.213 |
| R-free | 0.25600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dan |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.600 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNX (2000.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.127 | 0.410 |
| Number of reflections | 14974 | |
| <I/σ(I)> | 12 | 3.4 |
| Completeness [%] | 99.6 | 98.7 |
| Redundancy | 4.5 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 292 | PEG 10K, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
