5CM2

Structure of Y. lipolytica Trm9-Trm112 complex, a methyltransferase modifying U34 in the anticodon loop of some tRNAs

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SOLEIL BEAMLINE PROXIMA 1
Synchrotron site	SOLEIL
Beamline	PROXIMA 1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2012-05-11
Detector	PSI PILATUS 6M
Wavelength(s)	0.9801
Spacegroup name	I 4 3 2
Unit cell lengths	176.200, 176.200, 176.200
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.050 - 2.500
R-factor	0.201
Rwork	0.199
R-free	0.24200
Structure solution method	MAD
RMSD bond length	0.009
RMSD bond angle	1.193
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	SHARP
Refinement software	PHENIX (1.8.4_1496)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.650
High resolution limit [Å]	2.494	2.500
Rmerge		0.501
Number of reflections	16239
<I/σ(I)>	14.2	2.5
Completeness [%]	97.9	98.3
Redundancy	4.85	4.85

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	100MM TRI-SODIUM CITRATE, 20% POLYETHYLENE GLYCOL 4000 (PEG4K), 20% 2-PROPANOL, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	100MM TRI-SODIUM CITRATE, 20% POLYETHYLENE GLYCOL 4000 (PEG4K), 20% 2-PROPANOL, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K