5DU3
Active form of human C1-inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-02-07 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.953 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 57.410, 75.380, 203.960 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 57.400 - 2.100 |
| R-factor | 0.20818 |
| Rwork | 0.206 |
| R-free | 0.25697 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2oay |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.066 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0131) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.400 | 2.160 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.065 | |
| Rpim | 0.042 | 0.431 |
| Number of reflections | 52693 | |
| <I/σ(I)> | 14 | 1.6 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 4.7 | |
| CC(1/2) | 0.998 | 0.622 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 20% PEG3350 w/v and 200 mM KF with a crystallization drop size of 1 microlitre and a protein content of 70% w/v |
