8JSC
Structure of the FSP1 protein from Human
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL02U1 |
| Synchrotron site | SSRF |
| Beamline | BL02U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-08-24 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.820, 39.126, 70.345 |
| Unit cell angles | 90.00, 108.95, 90.00 |
Refinement procedure
| Resolution | 39.500 - 2.160 |
| R-factor | 0.1884 |
| Rwork | 0.187 |
| R-free | 0.22670 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.282 |
| Data reduction software | XDS |
| Data scaling software | ADDREF |
| Phasing software | PHENIX (v1.13) |
| Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 62.250 | 2.270 |
| High resolution limit [Å] | 2.160 | 2.160 |
| Number of reflections | 18472 | 2689 |
| <I/σ(I)> | 4.1 | |
| Completeness [%] | 99.4 | |
| Redundancy | 3.6 | |
| CC(1/2) | 0.972 | 0.556 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289.15 | PEG 3350, Ammonium nitrate. |






