6XI4

Crystal structure of Maf domain of human N-acetylserotonin O-methyltransferase-like protein soaked with TFBQ

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2018-02-01
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 2 21 21
Unit cell lengths	52.616, 84.507, 116.673
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.690 - 2.220
R-factor	0.2337
Rwork	0.233
R-free	0.25610
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2p5x
RMSD bond length	0.003
RMSD bond angle	0.680
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHENIX
Refinement software	PHENIX (1.15_3448)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.260
High resolution limit [Å]	2.220	2.220
Rmerge	0.084	1.167
Rpim	0.035	0.548
Number of reflections	26360	1235
<I/σ(I)>	33.22	1.9
Completeness [%]	99.4
Redundancy	6.8
CC(1/2)		0.522

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	298	0.1 M Hepes pH 7, 10% (w/v) PEG 5K MME, 5% tacsimate, 2.5 mM MgCl2 and 0.2 mM CoCl2. 10 mM of TFBQ was added to the crystallization drop and let to soak for 2.5 hours