1N28
Crystal structure of the H48Q mutant of human group IIA phospholipase A2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-05-20 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.933 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 119.580, 34.420, 73.900 |
| Unit cell angles | 90.00, 126.56, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.500 |
| Rwork | 0.184 |
| R-free | 0.27320 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.580 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.089 * | |
| Total number of observations | 161166 * | |
| Number of reflections | 37032 * | |
| Completeness [%] | 83.6 * | 79.1 |
| Redundancy | 2.4 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.4 | 4 * | NaCl, CaCl2, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Ca2+ | 5 (mM) | |
| 3 | 1 | drop | Tris-HCl | 0.1 (M) | pH7.4 |
| 4 | 1 | drop | 5.3 (M) | ||
| 5 | 1 | drop | octyl-beta-glucoside | 0.5 (mM) | |
| 6 | 1 | reservoir | PEG550 MME |
