1FAZ
THE CRYSTAL STRUCTURE OF PROKARYOTIC PHOSPHOLIPASE A2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 29.410, 57.750, 31.710 |
Unit cell angles | 90.00, 111.48, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.400 |
R-factor | 0.188 |
Rwork | 0.188 |
R-free | 0.23100 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.200 |
Phasing software | PHASES |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 1.450 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.074 | 0.276 |
Total number of observations | 22015 * | |
Number of reflections | 15558 | |
<I/σ(I)> | 34.2 | |
Completeness [%] | 77.5 | 61.1 |
Redundancy | 1.41 | 1.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 * | 297 * | PEG 4000, lithium sulfate, sodium cacodylate, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | Tris-HCl | 10 (mM) | |
2 | 1 | drop | 20 (mM) | ||
3 | 1 | drop | protein | 20 (mg/ml) | |
4 | 1 | reservoir | PEG6000 | 14 (%(w/v)) | |
5 | 1 | reservoir | 0.2 (M) | ||
6 | 1 | reservoir | sodium cacodylate | 0.1 (M) |