6EN7
Crystal structure of the ribosome assembly factor Nsa1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-05-19 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.987 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.723, 81.100, 87.574 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.408 - 2.403 |
R-factor | 0.1801 |
Rwork | 0.178 |
R-free | 0.21980 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5sum |
RMSD bond length | 0.002 |
RMSD bond angle | 0.516 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 59.500 | 2.489 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.044 | 0.113 |
Number of reflections | 15750 | 1543 |
<I/σ(I)> | 34.78 | 14.02 |
Completeness [%] | 99.9 | 99.23 |
Redundancy | 7.1 | 5.6 |
CC(1/2) | 0.999 | 0.992 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 294 | 0.1 M MES pH 6.5, 25% w/v PEG-1000 |