1ZJH
Structure of human muscle pyruvate kinase (PKM2)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-04-20 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 86.450, 111.290, 126.297 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.110 - 2.200 |
R-factor | 0.231 |
Rwork | 0.231 |
R-free | 0.27900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pkm |
RMSD bond length | 0.007 |
RMSD bond angle | 1.100 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.110 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.048 | 0.568 |
Number of reflections | 31389 | |
Completeness [%] | 99.9 | 100 |
Redundancy | 5.06 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291 | PEG 3350, Bis-Tris, ammonium acetate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |