3RUN
New strategy to analyze structures of glycopeptide antibiotic-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 | 2011-03-25 |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 60.440, 60.440, 96.830 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.784 - 1.400 |
| R-factor | 0.1491 |
| Rwork | 0.147 |
| R-free | 0.17990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2lzm |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.317 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.6.2_432) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 19.800 | 1.440 | |
| High resolution limit [Å] | 1.400 | 6.260 | 1.400 |
| Rmerge | 0.076 | 0.042 | 0.652 |
| Rmeas | 0.047 | 0.745 | |
| Number of reflections | 77081 | 850 | 5100 |
| <I/σ(I)> | 13.75 | 37.38 | 2.04 |
| Completeness [%] | 98.8 | 97.1 | 87.7 |
| Redundancy | 5.48 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 0.2M ammonium phosphate, 0.1M Tris 8.5, 35% MPD, vapor diffusion, hanging drop, temperature 291K |
