3HSH
Crystal structure of human collagen XVIII trimerization domain (Tetragonal crystal form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-06-24 |
Detector | NOIR-1 |
Wavelength(s) | 1.106 |
Spacegroup name | P 4 21 2 |
Unit cell lengths | 71.745, 71.745, 134.723 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.524 - 1.800 |
R-factor | 0.1795 |
Rwork | 0.175 |
R-free | 0.22430 |
Structure solution method | MOLECULAR REPLACEMENT |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHENIX |
Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.090 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.063 | 0.440 |
Number of reflections | 33455 | |
<I/σ(I)> | 24.5 | 5.5 |
Completeness [%] | 100.0 | 100 |
Redundancy | 11.9 | 9.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 3.5 | 298 | 1.65M ammonium sulfate, 0.1M citric acid, pH 3.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |