3Q3I
Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase in the presence of peptide N1131
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-07-16 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 79.701, 93.262, 176.705 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.970 - 2.450 |
R-factor | 0.181 |
Rwork | 0.178 |
R-free | 0.24300 |
Structure solution method | SIR |
RMSD bond length | 0.021 |
RMSD bond angle | 1.933 |
Data reduction software | HKL-3000 |
Data scaling software | SCALEPACK |
Phasing software | SHELX |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.540 |
High resolution limit [Å] | 2.450 | 2.450 |
Rmerge | 0.080 | 0.303 |
Number of reflections | 46099 | |
Completeness [%] | 94.1 | 83.1 |
Redundancy | 4.1 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 288 | 0.1 M MES, 0.1-0.16 M ammonium sulfate, 20-30% w/v PEG8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 288K |