1RMQ
Crystal structure of AphA class B acid phosphatase/phosphotransferase with osmiate mimicking the catalytic intermediate
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-02-12 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.13980, 1.14057, 1.13800 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 91.732, 66.447, 91.523 |
| Unit cell angles | 90.00, 121.30, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.000 |
| R-factor | 0.18661 |
| Rwork | 0.183 |
| R-free | 0.23002 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1n8n |
| RMSD bond length | 0.026 |
| RMSD bond angle | 1.943 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.580 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.089 | 0.402 |
| Number of reflections | 31710 | |
| <I/σ(I)> | 6.2 | 1.6 |
| Completeness [%] | 99.3 | 97.6 |
| Redundancy | 3.4 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 293 | AphA 6mg/mL, 50mM Na acetate, 25% PEG 6000, 10mM osmiate, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
