2BAX
Atomic Resolution Structure of the Double Mutant (K53,56M) of Bovine Pancreatic Phospholipase A2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X9B |
| Synchrotron site | NSLS |
| Beamline | X9B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-06-15 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 46.057, 46.057, 101.138 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 1.100 |
| R-factor | 0.114 |
| Rwork | 0.119 |
| R-free | 0.15600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1c74 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 0.028 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.140 |
| High resolution limit [Å] | 1.100 | 1.100 |
| Rmerge | 0.044 | 0.216 |
| Number of reflections | 50297 | |
| Completeness [%] | 98.2 | 99 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.2 | 293 | The double mutant protein was dissolved in 50 mM Tris buffer (7.2) containing 5mM of CaCl2, to a final protein Concentration of 17-20 mg/ml. The crystallization droplet contained 5 micro litre of protein and 2 micro litre of 60% MPD and the reservior contianined 1000 micro litre of 70% MPD, VAPOR DIFFUSION, temperature 293K |
