5VRC

Crystal structure for Methylobacterium extorquens PqqC (truncation of natural CD 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	2015-07-18
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	1.0332
Spacegroup name	P 21 21 21
Unit cell lengths	62.501, 114.185, 145.403
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.510 - 2.000
R-factor	0.19918
Rwork	0.197
R-free	0.23634
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1otv
RMSD bond length	0.028
RMSD bond angle	2.457
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall
Low resolution limit [Å]	29.510
High resolution limit [Å]	2.000
Rmerge	0.077
Number of reflections	69169
<I/σ(I)>	14.4
Completeness [%]	97.8
Redundancy	6.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		292	500 microL well volumes. Drops suspended on siliconized glass. Protein solution: 8.0 mg/mL protein in buffer (50 mM Tris, pH 8.0, 200mM sodium chloride). Well solution: 100 mM HEPES, pH 8.07, 200 mM sodium chloride, and 23.75% w/v PEG-3350. All water used in well solution buffers was 0.55 mM sodium azide for fungal growth suppression. Protein:well solution was 1:1 (1 microL to 1 microL)