1ZIN
ADENYLATE KINASE WITH BOUND AP5A
Experimental procedure
Source type | ROTATING ANODE |
Source details | SIEMENS |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1996-02-02 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 41.170, 62.338, 41.600 |
Unit cell angles | 90.00, 116.74, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.600 |
R-factor | 0.173 |
Rwork | 0.173 |
R-free | 0.21600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | YEAST ADENYLATE KINASE |
RMSD bond length | 0.011 |
RMSD bond angle | 22.621 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | |
High resolution limit [Å] | 1.600 | |
Rmerge | 0.097 | |
Number of reflections | 23448 | |
Completeness [%] | 97.0 | 81.5 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7 | 20 * | AMMONIUM SULFATE/PEG 1000, pH 7.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 10-30 (mg/ml) | |
2 | 1 | 1 | ammonium sulfate | 2.45 (M) | |
3 | 1 | 1 | PEG1000 | 1 (%) | or PEG750 monomethyl ether |
4 | 1 | 1 | HEPES | 50 (mM) | |
5 | 1 | 1 | sodium azide | 0.1 (%) | |
6 | 1 | 1 | Ap5A | 2-5 (mM) |