1QFX
PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM1A |
Synchrotron site | ESRF |
Beamline | BM1A |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 1997-01-29 |
Detector | MARRESEARCH |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 170.600, 170.600, 201.150 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.000 - 2.400 |
R-factor | 0.18 * |
Rwork | 0.183 |
R-free | 0.22500 |
Structure solution method | SIRAS |
RMSD bond length | 0.011 |
RMSD bond angle | 1.600 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | SHELXS |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.500 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.055 * | 0.182 * |
Total number of observations | 173451 * | |
Number of reflections | 58656 | |
<I/σ(I)> | 18.8 | 4.2 |
Completeness [%] | 86.5 | 67.3 |
Redundancy | 2.9 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | 0.1M HEPES/HCL PH 7.0, 2.4M AMMONIUM SULFATE |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 2.4 (M) | |
3 | 1 | reservoir | HEPES | 100 (mM) |