6N56

Crystal structure of fumarate reductase, flavo protein subunit, from Helicobacter pylori G27

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	2018-06-28
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 41 21 2
Unit cell lengths	63.890, 63.890, 354.530
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.464 - 2.350
R-factor	0.1744
Rwork	0.171
R-free	0.22240
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2BS2 as per MoRDa
RMSD bond length	0.007
RMSD bond angle	0.814
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MoRDa
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.464	47.464	2.410
High resolution limit [Å]	2.350	10.510	2.350
Rmerge	0.070	0.037	0.595
Rmeas	0.073	0.040	0.619
Total number of observations	386236
Number of reflections	31955	437	2289
<I/σ(I)>	23.75	49.66	4.77
Completeness [%]	99.4	90.3	100
Redundancy	12.087	8.783	12.475
CC(1/2)	0.999	0.998	0.949

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	20.9 mg/mL HepyC.18004.a.B1.PS38425 against Molecular dimensions Morpheus screen, D9 (10% PEG20000, 20% PEG550 MME, 20 mM 1,6-hexanediol, 20 mM 1-butanol, 20 mM (RS)-1,2- propanediol 2-propanol, 20 nM 1,4-butanediol, 20 mM 1,3-propanediol, 100 mM Bicine/Trizma base, pH 8.5), direct cryoprotection, tray 300244d9, puck ipi5-8