2ARU
Crystal structure of lipoate-protein ligase A bound with ATP
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 6B |
Synchrotron site | PAL/PLS |
Beamline | 6B |
Detector technology | CCD |
Collection date | 2004-12-08 |
Detector | BRUKER PROTEUM 300 |
Wavelength(s) | 1.0000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 108.532, 62.809, 46.448 |
Unit cell angles | 90.00, 111.34, 90.00 |
Refinement procedure
Resolution | 19.690 - 2.500 |
R-factor | 0.204 |
Rwork | 0.204 |
R-free | 0.25800 |
Structure solution method | MAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.700 |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 10079 | |
Completeness [%] | 98.8 | 93.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 100mM sodium citrate at pH 5.5, 20%(v/v) iso-propanol, 20%(w/v) PEG 3350, 100mM NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K |