1VDF
ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | ELLIOTT |
| Temperature [K] | 279 |
| Detector technology | IMAGE PLATE |
| Collection date | 1994-12-12 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.470, 49.470, 54.980 |
| Unit cell angles | 90.00, 103.84, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.050 |
| Rwork | 0.176 |
| Structure solution method | MIRAS |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.430 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MLPHARE |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.110 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.040 | |
| Total number of observations | 46638 * | |
| Number of reflections | 12978 | |
| <I/σ(I)> | 10.5 | 3.9 |
| Completeness [%] | 97.0 | 81 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 * | Efimov, V.P., (1996) Proteins: Struct.,Funct., Genet., 24, 259. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG1500 | 16-17 (%) | |
| 2 | 1 | reservoir | 0.5 (M) | ||
| 3 | 1 | reservoir | sodium phosphate | 50 (mM) | |
| 4 | 1 | drop | protein | 13 (mg/ml) | |
| 5 | 1 | drop | Tris-HCl | 10 (mM) | |
| 6 | 1 | drop | 200 (mM) | ||
| 7 | 1 | drop | PEG1500 | 16-17 (%) | |
| 8 | 1 | drop | 0.5 (M) | ||
| 9 | 1 | drop | sodium phosphate | 50 (mM) |
