3GRP
2.1 Angstrom crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase from Bartonella henselae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-02-05 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 59.279, 71.738, 111.521 |
| Unit cell angles | 90.00, 96.59, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.090 |
| R-factor | 0.195 |
| Rwork | 0.192 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Swiss Model |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.164 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.140 |
| High resolution limit [Å] | 2.090 | 2.090 |
| Rmerge | 0.069 | 0.507 |
| Number of reflections | 54858 | |
| <I/σ(I)> | 10.9 | |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 3.7 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 10 | 289 | 100 mM SPG buffer pH 10.0, 25% PEG 1500, 0.1 mg/mL Chymotrypsin, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
