6S6Y

X-ray crystal structure of the formyltransferase/hydrolase complex (FhcABCD) from Methylorubrum extorquens in complex with methylofuran

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X10SA
Synchrotron site	SLS
Beamline	X10SA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-11-16
Detector	DECTRIS PILATUS 6M
Wavelength(s)	1.00005
Spacegroup name	P 1
Unit cell lengths	84.974, 130.322, 172.689
Unit cell angles	84.97, 75.91, 82.09

Refinement procedure

Resolution	24.949 - 3.100
R-factor	0.2227
Rwork	0.221
R-free	0.25130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5t5i
Data reduction software	XDS
Data scaling software	SCALA (3.3.22)
Phasing software	PHASER
Refinement software	PHENIX (1.14_3260)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.500	48.502	3.270
High resolution limit [Å]	3.100	9.800	3.100
Rmerge	0.149	0.021	1.286
Rmeas	0.209	0.030	1.811
Rpim	0.147	0.021	1.275
Number of reflections	124496	3869	18285
<I/σ(I)>	5.2	28.8	0.6
Completeness [%]	96.6	94.7	96.9
Redundancy	1.8	1.8	1.8
CC(1/2)	0.983		0.308

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.7	292	The best hit was obtained in a CombiClover Junior Plate by using the sitting drop vapor diffusion method. 2 ul protein was mixed with 1 ul of the crystallization solution containing 0.2 M CaCl2 and 20% (w/v) PEG 3350. The protein buffer contained 25 mM Tris pH 7.7, 10% (v/v) glycerol, 2 mM DTT, 6 mM KCl and 200 mM NaCl.