2R0K
Protease domain of HGFA with inhibitor Fab58
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-04-05 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 188.658, 75.610, 69.139 |
| Unit cell angles | 90.00, 92.67, 90.00 |
Refinement procedure
| Resolution | 50.000 - 3.510 |
| R-factor | 0.25354 |
| Rwork | 0.251 |
| R-free | 0.31197 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | pdb 1YBW pdb 1FVD |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.190 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.630 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Rmerge | 0.128 | 0.300 |
| Number of reflections | 10827 | |
| <I/σ(I)> | 6.8 | 2.5 |
| Completeness [%] | 88.0 | 85.5 |
| Redundancy | 2.8 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 1:1 mixture of protein complex solution and reservoir containing 1.0M K/Na tartrate, CHES pH9.5, 0.2M Lithium Sulfate, VAPOR DIFFUSION, SITTING DROP |
