1ZUH
Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL12B2 |
Synchrotron site | SPring-8 |
Beamline | BL12B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-07-12 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0 |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 94.494, 94.494, 39.299 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.800 |
R-factor | 0.213 |
Rwork | 0.210 |
R-free | 0.26600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1via |
RMSD bond length | 0.021 |
RMSD bond angle | 1.992 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 67.420 | 1.850 |
High resolution limit [Å] | 1.790 | 1.790 |
Rmerge | 0.043 | 0.395 |
Number of reflections | 17190 | |
Completeness [%] | 98.9 | 89.9 |
Redundancy | 11.6 | 11 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | lithium sulfate,PEG 8000, sodium acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |