1K53
Monomeric Protein L B1 Domain with a G15A Mutation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-04-21 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 66.511, 66.511, 109.192 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.000 * - 2.100 |
R-factor | 0.213 * |
Rwork | 0.213 |
R-free | 0.23000 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1hz5 |
RMSD bond length | 0.006 * |
RMSD bond angle | 1.280 * |
Data scaling software | SCALEPACK |
Phasing software | EPMR |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.150 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.109 | 0.428 |
Total number of observations | 109046 * | |
Number of reflections | 16901 | |
<I/σ(I)> | 14.6 | 3.3 |
Completeness [%] | 99.9 | 100 |
Redundancy | 6.5 | 14.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 * | 277 | 225mM ZnOAC, 50mM Cacadylate pH6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | 50 (mM) | pH4.5 | |
2 | 1 | drop | 150 (mM) | ||
3 | 1 | drop | EDTA | 2 (mM) | |
4 | 1 | reservoir | 225 (mM) | ||
5 | 1 | reservoir | cacodylate | 50 (mM) | pH6.5 |