4N3B
Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26)E10Q and UDP-5SGlcNAc
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2012-11-01 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.1 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 98.910, 98.910, 364.931 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 49.592 - 2.170 |
R-factor | 0.1937 |
Rwork | 0.192 |
R-free | 0.22280 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.003 |
RMSD bond angle | 0.730 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA (3.3.20) |
Phasing software | PHENIX |
Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 85.658 | 52.133 | 2.290 |
High resolution limit [Å] | 2.170 | 6.880 | 2.170 |
Rmerge | 0.063 | 0.762 | |
Total number of observations | 15024 | 37832 | |
Number of reflections | 56847 | ||
<I/σ(I)> | 11.5 | 8.2 | 1 |
Completeness [%] | 99.9 | 99.8 | 99.5 |
Redundancy | 7.6 | 7.1 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 1.4M Sodium Malonate, 0.1M Bis Tris Propane, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |