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 |