3PBK
Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila
Replaces: 3GQWExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-03-12 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 91.469, 118.336, 137.973 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 89.824 - 3.000 |
| R-factor | 0.193 |
| Rwork | 0.190 |
| R-free | 0.25080 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3e53 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.067 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 89.824 | 3.050 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.198 | 0.648 |
| Number of reflections | 30776 | |
| <I/σ(I)> | 10.9 | 4 |
| Completeness [%] | 99.7 | 98.9 |
| Redundancy | 13.4 | 12.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 20% PEG 3350, 0.2 M Sodium fluoride, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
