1H4R
Crystal Structure of the FERM domain of Merlin, the Neurofibromatosis 2 Tumor Suppressor Protein.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X9B |
| Synchrotron site | NSLS |
| Beamline | X9B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-03-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 87.018, 89.328, 96.764 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 5.000 * - 1.800 |
| R-factor | 0.193 * |
| Rwork | 0.193 |
| R-free | 0.22700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1GC6.PDB |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.390 * |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.0.36) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 * | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.065 | 0.622 * |
| Number of reflections | 68222 * | 6875 * |
| <I/σ(I)> | 16.8 | 2.33 |
| Completeness [%] | 95.4 * | 97.2 |
| Redundancy | 3.6 * | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 6.5 | 294 * | THE PROTEIN WAS CRYSTALLIZED USING HANGING-DROP VAPOR DIFFUSION WIHTH 56% AMMONIUM SULFATE, 2% DIOXANE, 100 MM CACODYLATE, PH 6.5. A 1:1 RATIO OF PROTEIN TO WELL SOLUTION WAS USED. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 56 (%saturated) | |
| 3 | 1 | reservoir | dioxane | 2 (%) | |
| 4 | 1 | reservoir | sodium cacodylate | 0.1 (M) |
