3PGS
Phe3Gly mutant of EcFadL
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-09-10 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 63.068, 147.513, 151.092 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.778 - 1.900 |
| R-factor | 0.1671 |
| Rwork | 0.167 |
| R-free | 0.19150 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1t16 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.099 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: dev_572)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.000 | 1.880 |
| High resolution limit [Å] | 1.849 | 1.849 |
| Rmerge | 0.071 | 0.818 |
| Number of reflections | 119844 | |
| <I/σ(I)> | 24.3 | 1.9 |
| Completeness [%] | 99.0 | 98.5 |
| Redundancy | 5.3 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 295 | 0.1M NaOAc pH 5.5, 8.8 w/v PEG 2000 MME. Protein dialyzed in Tris buffer, C8E4 prior to setup, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
