1GPZ
THE CRYSTAL STRUCTURE OF THE ZYMOGEN CATALYTIC DOMAIN OF COMPLEMENT PROTEASE C1R
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-11-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 99.300, 101.800, 122.400 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 12.000 - 2.900 |
| R-factor | 0.242 |
| Rwork | 0.242 |
| R-free | 0.29200 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1elv |
| RMSD bond length | 0.015 |
| RMSD bond angle | 26.200 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 |
| Phasing software | AMoRE |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 12.000 | 3.060 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.056 | 0.340 * |
| Number of reflections | 27235 | |
| <I/σ(I)> | 11 | 2.2 |
| Completeness [%] | 99.8 * | 99.8 |
| Redundancy | 5.1 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.4 * | 20 * | 1.5 M AMMONIUM SULFATE, 0.1M TAPS, PH 8.5, AT 20 DEG C. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 2-6 (mg/ml) | |
| 2 | 1 | drop | 145 (mM) | ||
| 3 | 1 | drop | triethanolamine-hydrochloride | 50 (mM) | pH7.4 |
| 4 | 1 | reservoir | ammonium sulfate | 1.5 (M) | |
| 5 | 1 | reservoir | TAPS | 100 (mM) | pH8.5 |
