9Q35
Fibrinogen domain dimer from human Fibrinogen-like protein 1 (FGL-1)
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 | PIXEL |
| Collection date | 2021-04-09 |
| Detector | DECTRIS PILATUS3 X 6M |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 90.012, 39.777, 65.766 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.140 - 1.740 |
| R-factor | 0.16691 |
| Rwork | 0.166 |
| R-free | 0.21498 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fzd |
| RMSD bond length | 0.001 |
| RMSD bond angle | 1.758 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0430) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.140 | 1.780 |
| High resolution limit [Å] | 1.740 | 1.740 |
| Rmerge | 0.094 | 0.630 |
| Number of reflections | 24297 | 1034 |
| <I/σ(I)> | 9.6 | 2.1 |
| Completeness [%] | 97.7 | 78.7 |
| Redundancy | 5.6 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 290 | 10% PEG8000, 8% ETHYLENE GLYCOL, 0.1 M HEPES, PH 7.5 |
