3FBY
The crystal structure of the signature domain of cartilage oligomeric matrix protein.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-02-11 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97945 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 192.242, 192.242, 145.681 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 39.000 - 3.150 |
| R-factor | 0.2054 |
| Rwork | 0.202 |
| R-free | 0.26630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1UX6 AND 1YO8 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.632 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP ((CCP4)) |
| Refinement software | REFMAC (5.5.0054) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.000 | 3.260 |
| High resolution limit [Å] | 3.150 | 3.150 |
| Rmerge | 0.133 | 0.880 |
| Number of reflections | 53862 | |
| <I/σ(I)> | 15.4 | 2.3 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 6 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 289 | 50mM Ammonium Sulfate, 0.05M Bis-Tris, 30% (v/v) Pentaerythritol ethoxylate (15/4 EO/OH), pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
