2D1P
crystal structure of heterohexameric TusBCD proteins, which are crucial for the tRNA modification
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-10-11 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.979521, 0.979829, 0.9830 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 141.392, 141.392, 135.686 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.150 |
R-factor | 0.2094 |
Rwork | 0.209 |
R-free | 0.24230 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHARP |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.230 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.076 | 0.253 |
Number of reflections | 74991 | |
<I/σ(I)> | 43.8 | 7.1 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 11.9 | 9.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 293 | 0.9-1.1M lithium sulfate, 9mM Mg-acetate, 45mM Na-cacodylate buffer (pH 6.8), 2.5% tert-butanol, and 10mM Tris-HCl buffer (pH8.5), VAPOR DIFFUSION, HANGING DROP, temperature 293K |