1RMT
Crystal structure of AphA class B acid phosphatase/phosphotransferase complexed with adenosine.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-12-07 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.96111 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 84.740, 66.704, 88.556 |
| Unit cell angles | 90.00, 117.13, 90.00 |
Refinement procedure
| Resolution | 74.540 - 1.400 |
| R-factor | 0.16906 |
| Rwork | 0.167 |
| R-free | 0.19908 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1n8n |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.558 |
| 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] | 75.419 | 1.480 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.099 | 0.452 |
| Number of reflections | 153897 | |
| <I/σ(I)> | 3.7 | 1.6 |
| Completeness [%] | 59.3 | |
| Redundancy | 3.4 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 293 | Crystallization components* AphA 6mg/mL, 50mM Na acetate, 25% PEG 6000, 10mM adenosine, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
