3G5T

Crystal structure of trans-aconitate 3-methyltransferase from yeast

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	2008-12-10
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97886
Spacegroup name	P 21 21 21
Unit cell lengths	36.834, 91.891, 104.269
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	34.470 - 1.119
R-factor	0.121
Rwork	0.120
R-free	0.13700
Structure solution method	SAD
RMSD bond length	0.030
RMSD bond angle	2.262
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	REFMAC (5.5.0066)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.160
High resolution limit [Å]	1.119	2.410	1.119
Rmerge	0.104	0.075	0.322
Number of reflections	134803
<I/σ(I)>	32.628		4.464
Completeness [%]	97.4	99.6	77.3
Redundancy	12.5	14.3	6.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		277	Protein solution (8 mg/ml MSE Protein, 0.040 M NaCl, 0.00024 M TCEP, 0.001 M SAM, 0.008 M Trans-aconitic acid, 0.0045 M HEPES pH 7.0) mixed in a 1:1 ratio with the Well solution (24% PEG 8000, 2% DMSO, 0.05 M HEPES pH 7.5). Cryoprotected with 23% PEG 8000, 2% DMSO, 0.001 M SAM, 0.0085 M Trans-aconitate, 0.05 M HEPES pH 7.5, 19% Ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 277K