1G7V
CRYSTAL STRUCTURES OF KDO8P SYNTHASE IN ITS BINARY COMPLEXES WITH THE MECHANISM-BASED INHIBITOR
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 90 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 0.98104, 0.98066, 0.97719 |
| Spacegroup name | I 2 3 |
| Unit cell lengths | 117.600, 117.600, 117.600 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.400 |
| R-factor | 0.225 |
| Rwork | 0.221 |
| R-free | 0.24200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.017 |
| RMSD bond angle | 2.400 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 * | 2.400 |
| High resolution limit [Å] | 2.230 * | 2.230 * |
| Rmerge | 0.091 | 0.143 |
| Number of reflections | 26690 | |
| <I/σ(I)> | 14 | |
| Completeness [%] | 70.6 * | 14.1 * |
| Redundancy | 3.6 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.2 * | 23 * | MES or MOPS 61mM pH 6.1, 25% v/v Glycerol, 20mg/mL protein in tris buffer, 30 microgram/mL inhibitor, 10% v/v PEG 400, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Tris-HCl | 0.1 (M) | |
| 2 | 1 | drop | beta-mercaptoethanol | 0.02 (%) | |
| 3 | 1 | drop | sodium azide | 0.02 (%) | |
| 4 | 1 | drop | protein | 45 (mg/ml) | |
| 5 | 1 | reservoir | MOPS | 61 (mM) | |
| 6 | 1 | reservoir | glycerol | 25 (%(v/v)) | |
| 7 | 1 | reservoir | PEG400 | 10 (%(v/v)) | |
| 8 | 1 | reservoir | inhibitor 2 | 0.053 (mM) |
