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 |
