5UUN

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)	1.033
Spacegroup name	P 21 21 21
Unit cell lengths	68.590, 70.640, 168.570
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.975 - 1.450
R-factor	0.1168
Rwork	0.117
R-free	0.13570
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3c8e chain A
RMSD bond length	0.009
RMSD bond angle	1.346
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((1.12_2829: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.970	1.502
High resolution limit [Å]	1.450	1.450
Rmerge	0.044	0.205
Rpim	0.012	0.066
Number of reflections	140421	11067
<I/σ(I)>	36.36	8.82
Completeness [%]	96.5	76.88
Redundancy	13.2	10.3
CC(1/2)	1.000	0.986

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Saro protein at 277 mM was incubated with 10 mM reduced glutathione for 50 minutes prior to setting up crystallization experiments. An equal volume of protein solution and reservoir were deposited by a TTP Labtech Mosquito in a SD2 crystallization plate and allowed to equilibrate. The crystals were self-cryoprotected by the reservoir of 4 M ammonium acetate.