1MZA
crystal structure of human pro-granzyme K
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-01-12 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 31.465, 78.158, 83.629 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 22.000 - 2.230 |
R-factor | 0.2407 |
Rwork | 0.235 |
R-free | 0.28450 * |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | granzyme B |
RMSD bond length | 0.007 |
RMSD bond angle | 1.435 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.310 |
High resolution limit [Å] | 2.230 * | 2.230 |
Rmerge | 0.125 | |
Total number of observations | 65669 * | |
Number of reflections | 23808 | |
Completeness [%] | 97.1 * | 95.1 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.4 | 291 | 1.6M sodium formate, 2.5mM 2-[N-morpholino]ethane-sulfonic acid, 50mM sodium chloride, pH 8.4, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | sodium formate | 3.2 (M) | pH8.4 |