5VRD

Crystal structure for Methylobacterium extorquens PqqCD (natural fusion)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	PIXEL
Collection date	2015-10-19
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	1.0332
Spacegroup name	P 41 21 2
Unit cell lengths	103.936, 103.936, 243.485
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	243.490 - 2.850
R-factor	0.2569
Rwork	0.253
R-free	0.32707
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1otv
RMSD bond length	0.018
RMSD bond angle	2.088
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	243.490
High resolution limit [Å]	2.850
Rmerge	0.062	0.597
Rpim	0.032	0.320
Number of reflections	31557
<I/σ(I)>	17
Completeness [%]	98.5
Redundancy	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		292	500 microL well volumes. Protein solution: 8.0 mg/mL protein, 50 mM Tris, pH 7.9, 100 mM sodium chloride, and 1 mM TCEP. Well solution: 100 mM HEPES, pH 6.7, 19% w/v PEG-4000, 10% isopropanol. Water used in the well solutions contained 0.55 mM sodium azide. Hanging drops were 1 microL protein solution and 1 microL well solution