4DZR

The crystal structure of protein-(glutamine-N5) methyltransferase (release factor-specific) from Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2012-02-16
Detector	ADSC QUANTUM 315
Wavelength(s)	0.97931, 0.97948
Spacegroup name	P 41 21 2
Unit cell lengths	61.766, 61.766, 122.379
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.883 - 2.551
R-factor	0.2097
Rwork	0.207
R-free	0.26890
Structure solution method	MAD
RMSD bond length	0.009
RMSD bond angle	1.204
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	SHELXD
Refinement software	PHENIX ((phenix.refine: 1.7.1_743))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	31.000	2.590
High resolution limit [Å]	2.550	2.550
Rmerge	0.071	0.692
Number of reflections	8235
<I/σ(I)>	28.8	2.2
Completeness [%]	99.4	100
Redundancy	4.5	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	0.2M calcium acetate hydrate, pH 7.5, 20% (w/v) PEG 3350, 0.0125mg/ml Trypsin, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K