1MD8
Monomeric structure of the active catalytic domain of complement protease C1r
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 77 |
Detector technology | CCD |
Collection date | 2001-04-09 |
Detector | MARRESEARCH |
Wavelength(s) | 0.979549 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 112.911, 49.459, 77.249 |
Unit cell angles | 90.00, 106.19, 90.00 |
Refinement procedure
Resolution | 50.000 * - 2.800 |
R-factor | 0.2035 |
Rwork | 0.198 |
R-free | 0.25450 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 24.600 * |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 99.000 | 2.870 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.065 * | 0.189 * |
Number of reflections | 25998 * | |
<I/σ(I)> | 7 | |
Completeness [%] | 98.9 | 99.9 |
Redundancy | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 20 * | ammonium sulfate, TAPS, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG6000 | 12-20 (%) | |
2 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |
3 | 1 | reservoir | glycerol | 20 (%) | or 5% PEG4000 |