5WH9
Structure of BH1999 gentisyl-coenzyme A thioesterase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | BRUKER AXS MICROSTAR |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-12-14 |
| Detector | Bruker Platinum 135 |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 2 2 21 |
| Unit cell lengths | 53.656, 80.758, 120.282 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.280 - 2.300 |
| R-factor | 0.2227 |
| Rwork | 0.221 |
| R-free | 0.26350 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bvq |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.965 |
| Data reduction software | SAINT |
| Data scaling software | PROTEUM PLUS |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 38.300 |
| High resolution limit [Å] | 2.300 |
| Number of reflections | 21470 |
| <I/σ(I)> | 13.7 |
| Completeness [%] | 90.0 |
| Redundancy | 2.46 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 290 | 100 mM MOPS buffer with 200 mM NaCl and an equal volume of 0.24 M malonate pH 5.8, 18% PEG 3350 |
