2YXH
Crystal structure of mazG-related protein from Thermotoga maritima
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 120 |
Detector technology | CCD |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.97905, 0.90000, 0.97945 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 74.829, 56.788, 61.615 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.21472 |
Rwork | 0.212 |
R-free | 0.26312 |
Structure solution method | MAD |
RMSD bond length | 0.030 |
RMSD bond angle | 2.186 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.073 | 0.258 |
Number of reflections | 18408 | |
Completeness [%] | 99.7 | 98.8 |
Redundancy | 6.6 | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.4 | 293 | 25% PEG3350, 0.2M MgAcetate, 0.1M Tris-HCl, pH8.4, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K |