4ZJU
Structure of a NADH-dependent enoyl-ACP reductase from Acinetobacter baumannii in complex with NAD
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-04-09 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.97856 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 71.020, 92.440, 93.830 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.915 - 1.200 |
| R-factor | 0.1252 |
| Rwork | 0.125 |
| R-free | 0.14200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nqz |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.269 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 5.370 | 1.230 |
| High resolution limit [Å] | 1.200 | 3.790 | 1.200 |
| Rmerge | 0.049 | 0.017 | 0.537 |
| Rmeas | 0.055 | 0.020 | 0.607 |
| Total number of observations | 463957 | ||
| Number of reflections | 96282 | 2064 | 7053 |
| <I/σ(I)> | 18.71 | 62.76 | 2.75 |
| Completeness [%] | 99.9 | 100 | 100 |
| Redundancy | 4.8 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 290 | Molecular Dimensions Morpheus screen, h12: Morpheus H12: 20mM each L-Na-Glutamate, Alanine (racemic), Glycine, Lysine HCl (racemic), Serine (racemic); 100mM Tris (base)/Bicine pH 8.5; 15% each MPD (racemic), PEG 1000, PEG 3350; AcbaC.00170.a.B1.PW37673 at 25mg/ml with 5mM NADH; tray 262582, puck oxi7-1 |
