1J2Z
Crystal structure of UDP-N-acetylglucosamine acyltransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-18B |
Synchrotron site | Photon Factory |
Beamline | BL-18B |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9794 |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 90.686, 90.686, 148.203 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 * - 2.100 |
R-factor | 0.222 |
Rwork | 0.222 |
R-free | 0.26400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1lxa |
RMSD bond length | 0.005 |
RMSD bond angle | 24.200 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 * | 2.210 |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 21519 * | |
<I/σ(I)> | 6.9 | 1.8 |
Completeness [%] | 99.1 * | 99.8 |
Redundancy | 10.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 297 | Lee, B.I., (2002) Acta Cryst., D58, 864. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) |