1VKQ
A re-determination of the structure of the triple mutant (K53,56,120M) of phospholipase A2 at 1.6A resolution using sulphur-SAS at 1.54A wavelength
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X9A |
| Synchrotron site | NSLS |
| Beamline | X9A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 46.050, 46.050, 101.580 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.960 - 1.600 |
| R-factor | 0.17893 |
| Rwork | 0.177 |
| R-free | 0.21658 |
| Structure solution method | SULPHUR-SAS |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.536 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.960 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.059 | 0.284 |
| Number of reflections | 17048 | |
| <I/σ(I)> | 50.1 | |
| Redundancy | 12.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | vapor diffusion method | 7.2 | 293 | 50 mM Tris Buffer, 70% MPD reservoir,17-20Mg/ml prot,5 mM CaCl2 and 60% MPD in the droplet, pH 7.2, vapor diffusion method, temperature 293.0K |
