4X92
Crystal structure of Lysosomal Phospholipase A2-S165A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-06-14 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97937 |
| Spacegroup name | F 41 3 2 |
| Unit cell lengths | 257.239, 257.239, 257.239 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 3.000 |
| R-factor | 0.19 |
| Rwork | 0.188 |
| R-free | 0.22030 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4x90 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.349 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 3.050 |
| High resolution limit [Å] | 3.000 | 8.090 | 3.000 |
| Rmerge | 0.217 | 0.078 | 0.930 |
| Rmeas | 0.230 | 0.086 | |
| Rpim | 0.098 | 0.036 | 0.428 |
| Total number of observations | 83833 | ||
| Number of reflections | 14922 | ||
| <I/σ(I)> | 3.9 | ||
| Completeness [%] | 98.7 | 93.1 | 100 |
| Redundancy | 5.6 | 5.2 | 5.6 |
| CC(1/2) | 0.993 | 0.605 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | 100 mM Na cacodylate pH 6.5, 10% PEG 8000, 200 mM Mg(CH3COO) in the presence of DOPC liposomes |
