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 |