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. |