1HM9
CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, GLMU, BOUND TO ACETYL COENZYME A AND UDP-N-ACETYLGLUCOSAMINE
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 | 2000-05-16 |
| Detector | MARRESEARCH |
| Spacegroup name | H 3 |
| Unit cell lengths | 89.509, 89.509, 278.753 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.140 - 1.750 |
| R-factor | 0.183 |
| Rwork | 0.183 |
| R-free | 0.21900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hm8 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 24.600 * |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.800 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.046 | 0.354 |
| Total number of observations | 187478 * | |
| Number of reflections | 82248 | 5926 |
| <I/σ(I)> | 12.3 | 1.9 |
| Completeness [%] | 97.9 | 96.4 |
| Redundancy | 2.3 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 20 * | 18 % PEG 400 (w/w), 300 mM CaCl2 50 mM NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP at 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 13 (mg/ml) | |
| 2 | 1 | reservoir | PEG400 | 26 (%(v/v)) | |
| 3 | 1 | reservoir | 50 (mM) | ||
| 4 | 1 | reservoir | 300 (mM) | pH8.0 |
