3ZD2
THE STRUCTURE OF THE TWO N-TERMINAL DOMAINS OF COMPLEMENT FACTOR H RELATED PROTEIN 1 SHOWS FORMATION OF A NOVEL DIMERISATION INTERFACE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 120 |
| Detector technology | PIXEL |
| Collection date | 2011-06-29 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.270, 46.880, 111.660 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 55.830 - 1.990 |
| R-factor | 0.2224 |
| Rwork | 0.221 |
| R-free | 0.24810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2uwn |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.970 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.11.4) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 55.830 | 2.040 |
| High resolution limit [Å] | 1.990 | 1.990 |
| Rmerge | 0.090 | 0.540 |
| Number of reflections | 16303 | |
| <I/σ(I)> | 11.2 | 2.9 |
| Completeness [%] | 96.6 | 90.6 |
| Redundancy | 6.2 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 36% (W/V) PEG 2000 MME, 0.1M MES PH 6.5 |
