3HM0
Crystal Structure of Probable Thioesterase from Bartonella henselae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-05-09 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9765 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 62.639, 87.853, 96.910 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.010 - 2.500 |
| R-factor | 0.209 |
| Rwork | 0.206 |
| R-free | 0.26800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2pzh |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.313 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.121 | 0.464 |
| Number of reflections | 18932 | |
| <I/σ(I)> | 13.5 | 2.25 |
| Completeness [%] | 99.4 | 96.9 |
| Redundancy | 5.7 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | Sparse matrix screen condition a9, 20% PEG 3350, 0.2 M ammonium chloride, 16 mg/mL protein, crystal tracking ID 202329a9, 0.1 mg/mL chymotrypsin, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
