1FXJ
CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-02-16 |
| Detector | MARRESEARCH |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 142.680, 142.680, 248.130 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.250 |
| Rwork | 0.234 |
| R-free | 0.27400 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 24.800 * |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | SHELXS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | |
| High resolution limit [Å] | 2.250 | |
| Rmerge | 0.039 | 0.310 * |
| Number of reflections | 44 | |
| <I/σ(I)> | 14 | |
| Completeness [%] | 97.0 | 76.8 * |
| Redundancy | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 6 | 20 * | drop consists of equal amounts of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 25 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 1.3-1.5 (M) | |
| 3 | 1 | reservoir | MES | 0.1 (M) | |
| 4 | 1 | reservoir | acetone | 4 (%(v/v)) |






