2V0I
Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-acetylglucosamine-1-phosphate Uridyltransferase (GlmU)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-11-01 |
Detector | ADSC CCD |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 107.808, 107.808, 233.876 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 119.520 - 1.890 |
R-factor | 0.194 |
Rwork | 0.193 |
R-free | 0.21000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2v0h |
RMSD bond length | 0.008 |
RMSD bond angle | 1.266 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.070 | 0.320 |
Number of reflections | 64262 | |
<I/σ(I)> | 37.9 | 4.5 |
Completeness [%] | 99.1 | 99.9 |
Redundancy | 9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | 1.2-1.8M AMMONIUM SULFATE, 2%PEG-400, 0.1M MES PH 5.2-6.1, 20 MM MGCL2, 10 MM UDP-GLCNAC |