2XMQ
Crystal structure of human NDRG2 protein provides insight into its role as a tumor suppressor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 4A |
| Synchrotron site | PAL/PLS |
| Beamline | 4A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 86.411, 88.897, 126.799 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.810 |
| R-factor | 0.2039 |
| Rwork | 0.201 |
| R-free | 0.25847 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qmq |
| RMSD bond length | 0.029 |
| RMSD bond angle | 2.332 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.900 |
| High resolution limit [Å] | 2.810 | 2.800 |
| Rmerge | 0.100 | 0.420 |
| Number of reflections | 24361 | |
| <I/σ(I)> | 19.1 | 4.5 |
| Completeness [%] | 99.6 | 99 |
| Redundancy | 6.6 | 6.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9% PEG 8000, 0.2 M CALCIUM ACETATE, 0.1 M SODIUM CACODYLATE (PH 6.4 TO 7.5). |
