2V66
Crystal Structure of the coiled-coil domain of Ndel1 (a.a. 58 to 169) C
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-02-24 |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 46.431, 73.221, 69.026 |
Unit cell angles | 90.00, 105.40, 90.00 |
Refinement procedure
Resolution | 18.000 - 2.100 |
R-factor | 0.236 |
Rwork | 0.233 |
R-free | 0.31000 |
Structure solution method | MAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.026 |
RMSD bond angle | 1.922 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHARP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.300 | 2.170 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.080 | 0.310 |
Number of reflections | 300363 | |
<I/σ(I)> | 5 | 2.2 |
Completeness [%] | 99.8 | 100 |
Redundancy | 11.5 | 12 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.8 | 4% PEG 8000, 50 MM SODIUM PHOSPHATE PH 6.8, 100 MM NACL. PROTEIN CONCENTRATION 20 MG/ML. CRYOBUFFER = RESERVOIR PLUS 17% PEG 400. |