1Q3N
Crystal structure of KDO8P synthase in its binary complex with substrate PEP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-04-23 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9797 |
Spacegroup name | I 2 3 |
Unit cell lengths | 118.441, 118.441, 118.441 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.000 - 2.700 |
R-factor | 0.2423 |
Rwork | 0.235 |
R-free | 0.26800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1d9e |
RMSD bond length | 0.007 |
RMSD bond angle | 1.209 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.680 |
High resolution limit [Å] | 2.620 | 2.620 |
Rmerge | 0.060 | 0.396 |
Number of reflections | 8169 | |
Completeness [%] | 96.3 | 94.6 |
Redundancy | 6 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 293 | PEG 4000, Glycrol, Tris-HCl , pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |