1QL6
THE CATALYTIC MECHANISM OF PHOSPHORYLASE KINASE PROBED BY MUTATIONAL STUDIES
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF |
Synchrotron site | ESRF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-11-07 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.560, 68.171, 112.475 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.400 |
Rwork | 0.240 |
R-free | 0.33000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2phk |
RMSD bond length | 0.013 |
RMSD bond angle | 0.042 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | |
High resolution limit [Å] | 2.400 | |
Rmerge | 0.048 * | 0.221 * |
Total number of observations | 40795 * | |
Number of reflections | 12745 | |
<I/σ(I)> | 10.1 | |
Completeness [%] | 86.6 | 78.5 * |
Redundancy | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.2 * | 14 * | pH 6.90 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | Phk gamma trnc | 10-12 (mg/ml) | |
10 | 1 | reservoir | HEPES/NaOH | 50 (mM) | |
11 | 1 | reservoir | 10 (mM) | ||
12 | 1 | reservoir | glycerol | 10 (%(v/v)) | |
13 | 1 | reservoir | dithiothreitol | 10 (mM) | |
14 | 1 | reservoir | 0.02 (%(w/v)) | ||
2 | 1 | drop | AMPPNP | 3 (mM) | |
3 | 1 | drop | HEPES/NaOH | 10 (mM) | |
4 | 1 | drop | glycerol | 2 (%(v/v)) | |
5 | 1 | drop | dithiothreitol | 10 (mM) | |
6 | 1 | drop | 0.02 (%(w/v)) | ||
7 | 1 | drop | EDTA | 0.1 (mM) | |
8 | 1 | drop | 10 (mM) | ||
9 | 1 | reservoir | PEG8000 | 5 (%(w/v)) |