1MG4
STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: WILD TYPE 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 | 2002-03-08 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9187 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 85.981, 29.621, 40.332 |
| Unit cell angles | 90.00, 101.33, 90.00 |
Refinement procedure
| Resolution | 20.000 * - 1.500* |
| R-factor | 0.15472 |
| Rwork | 0.153 |
| R-free | 0.18700 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mfw |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.700 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.084 | 0.286 |
| Total number of observations | 47701 * | |
| Number of reflections | 15460 | |
| <I/σ(I)> | 14.1 | 2.5 |
| Completeness [%] | 96.8 | 85.7 |
| Redundancy | 3.1 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5 | 21 * | CITRATE BUFFER, AMMONIUM SULFATE, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 294K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 1.8-2.0 (M) | |
| 3 | 1 | reservoir | sodium citrate | 0.1 (M) | pH5.0 |






