4EIT
Crystal structure of an enoyl-(acyl carrier protein) reductase from Bartonella henselae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-03-28 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.07806 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 122.360, 76.860, 171.950 |
| Unit cell angles | 90.00, 107.99, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.400 |
| R-factor | 0.1972 |
| Rwork | 0.196 |
| R-free | 0.22620 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3grk |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.484 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER (2.3.0) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.460 | |
| High resolution limit [Å] | 2.400 | 10.730 | 2.400 |
| Rmerge | 0.089 | 0.050 | 0.441 |
| Number of reflections | 59084 | 697 | 4292 |
| <I/σ(I)> | 10.42 | 20.88 | 3.14 |
| Completeness [%] | 99.1 | 96.1 | 98.6 |
| Redundancy | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | BaheA.00010.b.A1 PW26981 selenomethionine-labeled at 27.5 mg/mL against PACT screen condition B5, 0.1 M MIB pH 8.0, 25% PEG 1500 with 15% ethylene glycol as cryo-protectant, crystal tracking ID 232038b5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
