6JOM
Crystal structure of lipoate protein ligase from Mycoplasma hyopneumoniae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U1 |
Synchrotron site | SSRF |
Beamline | BL17U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-11-12 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.97894 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 100.322, 100.322, 155.587 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.150 - 2.450 |
R-factor | 0.204 |
Rwork | 0.201 |
R-free | 0.26830 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.753 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.540 |
High resolution limit [Å] | 2.450 | 5.280 | 2.450 |
Rmerge | 0.060 | 0.034 | 0.758 |
Rmeas | 0.062 | 0.036 | 0.785 |
Rpim | 0.016 | 0.009 | 0.193 |
Number of reflections | 31325 | 3375 | 3049 |
<I/σ(I)> | 13.4 | ||
Completeness [%] | 99.6 | 99.3 | 99.1 |
Redundancy | 14.9 | 15.1 | 14.9 |
CC(1/2) | 0.999 | 0.903 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4 | 289 | 0.2 M (NH4)2SO4, 0.1 M sodium acetate pH 4.0, 20% PEG 2000 MME |
2 |