1LWB
Crystal structure of prokaryotic phospholipase A2 at atomic resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 297 |
Detector technology | IMAGE PLATE |
Collection date | 1997 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 0.71073 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 29.340, 57.495, 31.807 |
Unit cell angles | 90.00, 111.07, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.050 |
R-factor | 0.103 * |
Rwork | 0.103 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1faz |
RMSD bond length | 0.022 |
RMSD bond angle | 2.500 * |
Phasing software | X-PLOR |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 0.954 |
High resolution limit [Å] | 0.923 | 0.923 |
Rmerge | 0.072 | 0.228 |
Number of reflections | 45532 | 1418 * |
<I/σ(I)> | 8.21 | 1.64 |
Completeness [%] | 67.5 | 22.75 |
Redundancy | 2.65 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 * | 297 | Matoba, Y., (2002) J.Biol.Chem., 277, 20059. * |
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) |