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 |