5A08
X-ray structure of the mannosyltransferase Ktr4p from S. cerevisiae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-05-17 |
Detector | DECTRIS PIXEL |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 60.198, 102.368, 156.908 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 85.740 - 2.210 |
R-factor | 0.16502 |
Rwork | 0.163 |
R-free | 0.20273 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1s4n |
RMSD bond length | 0.017 |
RMSD bond angle | 1.684 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.130 | 0.650 |
Number of reflections | 49674 | |
<I/σ(I)> | 13.8 | 3 |
Completeness [%] | 99.7 | 97 |
Redundancy | 7.8 | 8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 0.1M NA-CACODYLATE, PH 6.5 0.2M CAOAC 18% (W/V) PEG8000 |