6MC8

Crystal structure of PprA dimer from Deinococcus deserti

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2017-06-30
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.54056
Spacegroup name	P 21 21 21
Unit cell lengths	54.417, 80.985, 148.868
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.720 - 2.500
Rwork	0.247
R-free	0.26100
Structure solution method	MOLECULAR REPLACEMENT
Data reduction software	CrysalisPro (39.29c)
Data scaling software	Aimless (0.5.32)
Phasing software	PHASER (1.13-2998)
Refinement software	PHENIX (1.13-2998)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	28.720	2.600
High resolution limit [Å]	2.500	2.500
Rmerge	0.182	0.663
Rmeas	0.189	0.700
Rpim	0.049	0.223
Number of reflections	22737	2079
<I/σ(I)>	19.8	2
Completeness [%]	96.7	80.2
Redundancy	24.1	11.6
CC(1/2)	0.998	0.845

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	9.5	293.15	Protein at 3.0 mg/mL in 800 mM NaCl, 150 mM Imidazole, 20 mM Tris, pH 8.0 was mixed in 1:1 volume ratio with MCSG3 #92 - a solution of 30 % (w/v) PEG 400 and 0.1 M CHES, pH 9.5. The drop was suspended over 1.5M Ammonium sulfate.