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 |
