2P0L
Crystal structure of a Lipoate-protein ligase A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-02-27 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.97950 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 46.961, 49.245, 61.452 |
Unit cell angles | 90.00, 99.22, 90.00 |
Refinement procedure
Resolution | 40.060 - 2.040 |
R-factor | 0.231 |
Rwork | 0.231 |
R-free | 0.27300 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELXD |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.110 |
High resolution limit [Å] | 2.040 | 2.040 |
Rmerge | 0.096 | 0.414 |
Number of reflections | 17861 | |
<I/σ(I)> | 11.1 | 1 |
Completeness [%] | 99.5 | 96.1 |
Redundancy | 4.9 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | 0.1M Tris-HCl pH 8.5, 30% PEG4000, 0.2M MgCl2, VAPOR DIFFUSION, SITTING DROP, temperature 298K |