2IUC
Structure of alkaline phosphatase from the Antarctic bacterium TAB5
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-11-27 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 70.043, 173.184, 55.340 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.740 - 1.950 |
R-factor | 0.165 |
Rwork | 0.162 |
R-free | 0.22500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ed9 |
RMSD bond length | 0.027 |
RMSD bond angle | 1.934 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.060 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.130 | 0.260 |
Number of reflections | 48685 | |
<I/σ(I)> | 12.3 | 2.3 |
Completeness [%] | 97.3 | 84.3 |
Redundancy | 4.2 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | HANGING-DROP, 4 DEGREE C, 17 MG/ML PROTEIN, 23% PEG3350, 0.2M NAAC, 10MM 4-NITROPHENYL PHOSPHATE, 0.1M CACODYLATE, PH 6.5 |