6V45

Crystal structure of a Probable carnitine operon oxidoreductase caia from Brucella melitensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2019-10-30
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 2 3
Unit cell lengths	96.060, 96.060, 96.060
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	42.960 - 2.600
R-factor	0.2023
Rwork	0.199
R-free	0.23460
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	MR-rosetta based on PDB entries 4LZH_A 4A1K_A 3ZGP_A 6NTW_A 5E5L_A 1ZAT_A 6D5A_A 4XVO_B 4QRB_A 4Z7A_A
RMSD bond length	0.005
RMSD bond angle	0.708
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MR-Rosetta
Refinement software	PHENIX (1.17.1)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.670
High resolution limit [Å]	2.600	11.630	2.600
Rmerge	0.044	0.022	0.639
Rmeas	0.047	0.024	0.687
Number of reflections	9354	126	700
<I/σ(I)>	27.75	58.96	3
Completeness [%]	99.9	96.2	100
Redundancy	7.36	5.619	7.511
CC(1/2)	0.999	0.998	0.862

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	Optimization screen around condition Anatrace MCSG1_E6, well C4: 18.9% (w/V) PEG 3350, 200mM Potassium sulfate: BrmeA.18116.b.B2.PS01846 at 18.1mg/ml: tray 312854c4, cryo: 20% EG in 2 steps: puck xvm4-2.