1QMU
Duck carboxypeptidase D domain II
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 110 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 3 |
| Unit cell lengths | 135.540, 135.540, 135.540 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.700 |
| R-factor | 0.203 * |
| Rwork | 0.198 |
| R-free | 0.23600 |
| Structure solution method | SIRAS |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.590 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | CNS (0.4) |
| Refinement software | CNS (0.4) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.850 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.076 | 0.608 |
| Total number of observations | 270100 * | |
| Number of reflections | 22564 | |
| <I/σ(I)> | 8.3 | 1.2 |
| Completeness [%] | 98.0 | 87 |
| Redundancy | 12 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8 * | 20 * | pH 5.20 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 5 (mM) | |
| 3 | 1 | drop | 50 (mM) | ||
| 4 | 1 | drop | benzamidine | 0.5 (mM) | |
| 5 | 1 | reservoir | ammonium sulfate | 2.1 (M) | |
| 6 | 1 | reservoir | sodium acetate | 0.1 (M) |
