1X2G
Crystal Structure of Lipate-Protein Ligase A from Escherichia coli
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44XU |
Synchrotron site | SPring-8 |
Beamline | BL44XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-05-31 |
Detector | Bruker DIP-6040 |
Wavelength(s) | 0.9000 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 82.000, 112.800, 289.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.600 - 2.400 |
R-factor | 0.1742 |
Rwork | 0.171 |
R-free | 0.23337 |
Structure solution method | SAD |
RMSD bond length | 0.021 |
RMSD bond angle | 1.830 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.059 | 0.297 |
Number of reflections | 52725 | |
<I/σ(I)> | 18 | 2.92 |
Completeness [%] | 99.4 | 99.7 |
Redundancy | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | ethylene glycol, glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |