2B82
Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with adenosine and phosphate bound to the catalytic metal at 1.2 A resolution
Replaces: 1RMWExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-12-07 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.96111 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 90.971, 66.868, 86.120 |
| Unit cell angles | 90.00, 116.96, 90.00 |
Refinement procedure
| Resolution | 76.710 - 1.250 |
| R-factor | 0.16693 |
| Rwork | 0.165 |
| R-free | 0.18850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1n8n |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.391 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 76.710 | 1.320 |
| High resolution limit [Å] | 1.250 | 1.250 |
| Rmerge | 0.069 | 0.220 |
| Number of reflections | 112327 | |
| <I/σ(I)> | 5.1 | 3 |
| Completeness [%] | 88.7 | 58.2 |
| Redundancy | 2.6 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 293 | AphA 6mg/mL, 50 mM Na acetate, 25% PEG 6000, 10mM AMP, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
