3WRW
Crystal structure of the N-terminal domain of resistance protein
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL38B1 |
Synchrotron site | SPring-8 |
Beamline | BL38B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-07-21 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9788, 0.9792, 0.9639 |
Spacegroup name | P 1 |
Unit cell lengths | 77.970, 105.280, 110.620 |
Unit cell angles | 94.56, 109.27, 107.99 |
Refinement procedure
Resolution | 49.640 - 2.710 |
R-factor | 0.21059 |
Rwork | 0.207 |
R-free | 0.27781 |
Structure solution method | MAD |
RMSD bond length | 0.012 |
RMSD bond angle | 1.543 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AutoSol |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.640 | 2.860 |
High resolution limit [Å] | 2.710 | 2.710 |
Rmerge | 0.237 | |
Number of reflections | 79784 | |
<I/σ(I)> | 3.1 | |
Completeness [%] | 95.0 | 95.5 |
Redundancy | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 8.0% (W/v) PEG 8000, 0.4M ammonium tartrate dibasic, VAPOR DIFFUSION, HANGING DROP, temperature 293K |