1U9L
Structural basis for a NusA- protein N interaction
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
Synchrotron site | MPG/DESY, HAMBURG |
Beamline | BW6 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-08-11 |
Detector | MARRESEARCH |
Wavelength(s) | 0.95, 1.05 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 69.787, 69.787, 67.020 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.840 - 1.900 |
R-factor | 0.21659 |
Rwork | 0.216 |
R-free | 0.23700 |
Structure solution method | MAD |
RMSD bond length | 0.004 |
RMSD bond angle | 1.231 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELXS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.950 |
High resolution limit [Å] | 1.850 | 1.850 |
Number of reflections | 13388 | |
<I/σ(I)> | 17.8 | 1.3 |
Completeness [%] | 98.5 | 99.4 |
Redundancy | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 293 | Ammonium sulfate, MES, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |