6FRM

Crystal Structure of coenzyme F420H2 oxidase (FprA) co-crystallized with 10 mM Tb-Xo4

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-08-27
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	1.07227
Spacegroup name	P 1 21 1
Unit cell lengths	84.170, 147.875, 146.059
Unit cell angles	90.00, 90.40, 90.00

Refinement procedure

Resolution	48.690 - 2.200
R-factor	0.178
Rwork	0.177
R-free	0.20900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2ohh
RMSD bond length	0.010
RMSD bond angle	1.160
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	BUSTER (2.10.3)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.690	2.310
High resolution limit [Å]	2.190	2.190
Rpim	0.044	0.534
Number of reflections	181493
<I/σ(I)>	9
Completeness [%]	99.0
Redundancy	6.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		291	FprA native (about 90 % pure) at 43 g/l + 10 mM Xo4, crystallized at 291 K under anaerobic condition (95% N2 / 5% H2) in Combiclover Junior plate from Jena Bioscience. The protein was crystallized by mixing 1 ul protein of this mix with 1 ul of the mother liquor containing 20% w/v PEG 8000, 100 mM HEPES pH 7.5, 200 mM Ammonium sulfate and 10 % v/v 2-propanol. Prior to freezing in liquid nitrogen, the crystal was soaked for few seconds in a cryo-protected solution containing: 20% w/v PEG 8000, 100 mM HEPES pH 7.5, 200 mM Ammonium sulfate, 10 % v/v 2-propanol, 25 % v/v glycerol.