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