1E0U
Structure R271L mutant of E. coli pyruvate kinase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-02-15 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 74.010, 129.590, 241.770 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.800 |
R-factor | 0.245 |
Rwork | 0.245 |
R-free | 0.31200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pky |
RMSD bond length | 0.019 |
RMSD bond angle | 0.044 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 |
Phasing software | CCP4 |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.090 | 0.201 |
Total number of observations | 151954 * | |
Number of reflections | 56604 | |
<I/σ(I)> | 6.5 | 3.1 |
Completeness [%] | 97.7 | 86.1 |
Redundancy | 2.7 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 * | pH 6.20 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG4000 | 12 (%(w/v)) | |
2 | 1 | reservoir | 20 (mM) | ||
3 | 1 | reservoir | 20 (mM) | ||
4 | 1 | reservoir | MES | 50 (mM) |