1GO4
Crystal structure of Mad1-Mad2 reveals a conserved Mad2 binding motif in Mad1 and Cdc20.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF |
| Synchrotron site | ESRF |
| Temperature [K] | 287 |
| Detector technology | CCD |
| Collection date | 2001-05-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 111.037, 63.023, 139.511 |
| Unit cell angles | 90.00, 111.65, 90.00 |
Refinement procedure
| Resolution | 24.500 - 2.050 |
| R-factor | 0.24 |
| Rwork | 0.240 |
| R-free | 0.26800 |
| Structure solution method | SIRAS |
| Starting model (for MR) | 1duj |
| RMSD bond length | 0.015 * |
| RMSD bond angle | 1.880 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SnB |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.180 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.038 | 0.341 * |
| Total number of observations | 368557 * | |
| Number of reflections | 113010 | |
| <I/σ(I)> | 18.2 | 2.96 |
| Completeness [%] | 99.2 | 90 |
| Redundancy | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.2 | 20 * | PROTEIN CONCENTRATION 7.5 MG/ML HANGING DROP METHOD, WELL=100 MM AMMONIUM SULPHATE, 100 MM AMMONIUM CITRATE PH 5.2, 10 MM DTT |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 7.5 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 100 (mM) | |
| 3 | 1 | reservoir | sodium citrate | 100 (mM) | pH5.2 |
| 4 | 1 | reservoir | dithiothreitol | 10 (mM) |
