3R4C
Divergence of Structure and Function Among Phosphatases of the Haloalkanoate (HAD) Enzyme Superfamily: Analysis of BT1666 from Bacteroides thetaiotaomicron
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-03-16 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 52.765, 70.666, 72.426 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.107 - 1.820 |
| R-factor | 0.166 |
| Rwork | 0.164 |
| R-free | 0.19750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ymq |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.002 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.890 |
| High resolution limit [Å] | 1.820 | 1.820 |
| Rmerge | 0.108 | 0.557 |
| Number of reflections | 24886 | |
| <I/σ(I)> | 15.5 | 3 |
| Completeness [%] | 100 | |
| Redundancy | 7.2 | 7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 0.1 M Bis-Tris, 0.2 M ammonium sulfate, 25% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 6.5 |
