1ELV
CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COMPLEMENT C1S PROTEASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-09-24 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 39.080, 79.650, 60.210 |
Unit cell angles | 90.00, 91.24, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.700 |
R-factor | 0.185 * |
Rwork | 0.186 |
R-free | 0.21900 |
RMSD bond length | 0.020 |
RMSD bond angle | 0.024 |
Data reduction software | XDS |
Data scaling software | XDS |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.750 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.037 * | 0.247 * |
Total number of observations | 115710 * | |
Number of reflections | 39489 * | |
<I/σ(I)> | 16.9 | 3.4 |
Completeness [%] | 93.0 | 75.8 |
Redundancy | 2.9 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.4 | 4 * | PEG 4K 34%, AMMONIUM SULFATE 100mM, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6 (mg/ml) | |
2 | 1 | drop | TEA-HCl | 50 (mM) | |
3 | 1 | drop | 145 (mM) | ||
4 | 1 | reservoir | PEG4000 | 34 (%) | |
5 | 1 | reservoir | ammonium sulfate | 100 (mM) |