3MVA
Crystal structure of human MTERF1 bound to the termination sequence
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-08-21 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.09, 0.9195, 0.9197, 0.9000 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 88.631, 89.709, 161.293 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.987 - 2.200 |
R-factor | 0.208 |
Rwork | 0.205 |
R-free | 0.24400 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.243 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.240 |
High resolution limit [Å] | 2.200 | 5.970 | 2.200 |
Rmerge | 0.050 | 0.036 | 0.602 |
Number of reflections | 32806 | ||
<I/σ(I)> | 17.8 | ||
Completeness [%] | 99.2 | 87.7 | 99.1 |
Redundancy | 7.2 | 6.5 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 298 | PEG 3350, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |