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 |