1N29
Crystal structure of the N1A mutant of human group IIA phospholipase A2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-03-21 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 74.790, 74.790, 88.891 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 - 2.600 |
| Rwork | 0.242 |
| R-free | 0.31970 |
| 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] | 15.000 | 2.800 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.066 * | |
| Total number of observations | 31180 * | |
| Number of reflections | 4693 * | |
| Completeness [%] | 99.5 * | 99.8 |
| Redundancy | 3.4 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.5 | 4 * | NaCl, CaCl2, pH 7.5, 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) | pH7.5 |
| 4 | 1 | drop | 5.5 (M) | ||
| 5 | 1 | drop | octyl-beta-glucoside | 0.5 (mM) | |
| 6 | 1 | reservoir | PEG550 MME |
