3RUL
New strategy to analyze structures of glycopeptide-target complexes
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X6A |
Synchrotron site | NSLS |
Beamline | X6A |
Temperature [K] | 93 |
Collection date | 2010-03-02 |
Wavelength(s) | 0.9537 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 53.300, 86.250, 107.190 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.603 - 2.500 |
R-factor | 0.2445 |
Rwork | 0.243 |
R-free | 0.27740 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3anj |
RMSD bond length | 0.008 |
RMSD bond angle | 1.285 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX (1.6.2_432) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 19.600 |
High resolution limit [Å] | 2.500 |
Number of reflections | 16489 |
Completeness [%] | 93.1 |
Redundancy | 16 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | 24% PEG3350, 0.2M ammonium tartrate, 0.015M CYMAL-7, VAPOR DIFFUSION, HANGING DROP, temperature 291K |