2JF3
Nucleotide substrate binding by UDP-N-acetylglucosamine acyltransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-05-20 |
Detector | MARRESEARCH |
Spacegroup name | P 21 3 |
Unit cell lengths | 97.740, 97.740, 97.740 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 69.170 - 3.000 |
R-factor | 0.22 |
Rwork | 0.218 |
R-free | 0.27000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1lxa |
RMSD bond length | 0.006 |
RMSD bond angle | 0.940 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 69.170 | 3.160 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.110 | 0.340 |
Number of reflections | 6451 | |
<I/σ(I)> | 7.6 | 2.5 |
Completeness [%] | 99.8 | 100 |
Redundancy | 3.2 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 10% PEG 10000, 0.1M MES PH6.5, pH 6.50 |