4YYC

Crystal structure of trimethylamine methyltransferase from Sinorhizobium meliloti in complex with unknown ligand

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2014-11-06
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.07808
Spacegroup name	P 21 21 2
Unit cell lengths	89.162, 60.025, 88.345
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.560
R-factor	0.1403
Rwork	0.139
R-free	0.16540
Structure solution method	SAD
RMSD bond length	0.013
RMSD bond angle	1.563
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	HKL-3000
Refinement software	REFMAC (5.8.0107)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.590
High resolution limit [Å]	1.560	4.230	1.560
Rmerge	0.052	0.025	0.615
Rmeas	0.059	0.028	0.710
Rpim	0.027	0.013	0.344
Total number of observations	315705
Number of reflections	67995
<I/σ(I)>	10.3		1.9
Completeness [%]	99.3	97.2	97.4
Redundancy	4.6	4.5	3.8
CC(1/2)		0.999	0.806

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	289	0.2 ul of 14 mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 10% Glycerol, 0.1% Sodium Azide and 0.5 mM TCEP were mixed with 0.2 ul of the MCSG-I condition #33 (32%w/v PEG 4K, 0.1M Tris HCl, 0.8 M Lithium Chloride, pH=8.5) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci). Before crystallization protein was mixed with 1/15 v/v of 1 mg/ml TEV protease solution