1K50
A V49A Mutation Induces 3D Domain Swapping in the B1 Domain of Protein L from Peptostreptococcus magnus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-06-25 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 43 |
| Unit cell lengths | 53.134, 53.134, 115.514 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.140 - 1.800 |
| R-factor | 0.211 * |
| Rwork | 0.214 |
| R-free | 0.23900 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hz6 |
| RMSD bond length | 0.006 * |
| RMSD bond angle | 1.250 * |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.047 | 0.435 |
| Total number of observations | 134022 * | |
| Number of reflections | 29286 * | |
| <I/σ(I)> | 30.9 | 2.3 |
| Completeness [%] | 98.7 * | 93.3 |
| Redundancy | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 277 | 18% PEG3350, 0.2M (NH4)2SO4, 100mM Citrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | sodium phosphate | 15 (mM) | pH7.0 |
| 2 | 1 | reservoir | PEG3350 | 18 (%) | |
| 3 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
| 4 | 1 | reservoir | citrate | 100 (mM) | pH4.5 |
