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 |