1CNK
X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE
Experimental procedure
Detector technology | IMAGE PLATE |
Collection date | 1994-06-23 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.700, 41.700, 73.000 |
Unit cell angles | 90.00, 104.60, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.150 |
R-factor | 0.176 |
Rwork | 0.176 |
RMSD bond length | 0.011 |
RMSD bond angle | 25.900 * |
Data reduction software | MOSFLM |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 8.000 * |
High resolution limit [Å] | 2.150 * |
Rmerge | 0.067 |
Number of reflections | 18287 |
Completeness [%] | 92.0 |
Redundancy | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 8 * | 20 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | Tris-Cl | 50 (mM) | or Tris-SO4, pH8.0 |
2 | 1 | reservoir | ammonium sulfate | 50-70 (%saturated) | 1.75-2.5M |
3 | 1 | drop | protein | 0.3 (mM) | |
4 | 1 | drop | Tris-Cl | 50 (mM) | or Tris-SO4, pH8.0 |