5UUO
Crystal structure of SARO_2595 from Novosphingobium aromaticivorans
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-06-30 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.7749 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 68.810, 70.390, 168.230 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.810 - 1.250 |
R-factor | 0.1303 |
Rwork | 0.130 |
R-free | 0.13230 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.024 |
Data reduction software | XSCALE (May 1, 2016 BUILT=20160617) |
Data scaling software | XDS (VERSION Oct 15, 2015) |
Phasing software | PHASER (2.6.0) |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.360 | 1.280 |
High resolution limit [Å] | 1.250 | 1.250 |
Rmerge | 0.052 | 1.297 |
Rpim | 0.015 | 0.356 |
Number of reflections | 225442 | 16479 |
<I/σ(I)> | 21.85 | 1.96 |
Completeness [%] | 99.9 | 99.8 |
Redundancy | 13.5 | 13.9 |
CC(1/2) | 1.000 | 0.841 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | Saro protein at 277 mM was incubated with 10 mM reduced glutathione for 50 minutes prior to setting up crystallization experiments. The droplet yielding the crystal with the highest observed diffracting power was composed of 130 nL protein and 85 nL reservoir solution. The reservoir solution was 1.35 M ammonium sulfate, 0.1 M lithium sulfate 0.1 M bis-trispropane, pH 7.5 |