4AFN
Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (FabG) from Pseudomonas aeruginosa at 2.3A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-2 |
| Synchrotron site | MAX II |
| Beamline | I911-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-04 |
| Detector | MARRESEARCH |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 78.280, 111.170, 116.290 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.160 - 2.300 |
| R-factor | 0.20415 |
| Rwork | 0.201 |
| R-free | 0.26382 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ftp |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.739 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.160 | 2.420 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.120 | 0.510 |
| Number of reflections | 45767 | |
| <I/σ(I)> | 8.6 | 2.9 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 4.9 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.8 | 0.1 M TRIS-HCL PH 7.8, 10% (W/V)PEG 3350, PROTEIN CONCENTRATION 8MG/ML |
