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). |