5CRJ
Crystal Structure of the MTERF1 F322A substitution bound to the termination sequence.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-20 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.075 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 89.245, 90.136, 161.431 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 80.720 - 2.590 |
R-factor | 0.2108 |
Rwork | 0.208 |
R-free | 0.27600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3mva |
RMSD bond length | 0.011 |
RMSD bond angle | 1.593 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0071) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 161.431 | 2.598 |
High resolution limit [Å] | 2.589 | 2.589 |
Rmerge | 0.042 | 0.825 |
Number of reflections | 20665 | |
<I/σ(I)> | 29.1 | 2.5 |
Completeness [%] | 100.0 | 100 |
Redundancy | 7.2 | 7.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 0.2M Sodium Acetate, 0.1M Tris HCl pH 8.0, 15.5% Peg4000 |