1LF7
Crystal Structure of Human Complement Protein C8gamma at 1.2 A Resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 94 |
Detector technology | PIXEL |
Collection date | 1999-06-26 |
Detector | DECTRIS PILATUS3 X 6M |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 42.448, 58.993, 72.053 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.030 - 1.200 |
R-factor | 0.223 |
Rwork | 0.223 |
R-free | 0.22900 |
Structure solution method | MIRAS |
RMSD bond length | 0.004 |
RMSD bond angle | 1.100 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.240 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.043 | |
Number of reflections | 53030 | |
Completeness [%] | 92.2 | 63.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 * | 4 * | PEG 4000, sodium citrate, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | imidazole | 25 (mM) | |
2 | 1 | drop | 150 (mM) | pH7.2 | |
3 | 1 | drop | protein | 0.3-0.5 (mg/ml) | |
4 | 1 | reservoir | PEG4000 | 28-36 (%) | |
5 | 1 | reservoir | sodium citrate | 0.1 (M) | pH4.0 |