1N2X

Crystal Structure Analysis of TM0872, a Putative SAM-dependent Methyltransferase, Complexed with SAM

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 5ID-B
Synchrotron site	APS
Beamline	5ID-B
Temperature [K]	170
Detector technology	CCD
Collection date	2002-04-03
Detector	MARRESEARCH
Wavelength(s)	0.9785
Spacegroup name	P 21 3
Unit cell lengths	133.960, 133.960, 133.960
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 1.900
R-factor	0.205
Rwork	0.205
R-free	0.22600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1m6y
RMSD bond length	0.007
RMSD bond angle	1.200
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.079	0.386
Total number of observations	1623397 *
Number of reflections	63197 *
<I/σ(I)>	29	4.65
Completeness [%]	99.8	99.9
Redundancy	25.7	7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	4 *	DROP- 50 mM NA CACODYLATE pH 6.5, 5 mM HEPES pH 7.5, 0.1 M AMMONIUM SULFATE, 9 % PEG 8000, 0.25 M NACL, 1.0 MM BME, 10 MG/ML PROTEIN. WELL- 0.1M NA CACODYLATE pH 6.5, 0.1 M AMMONIUM SULFATE, 18 % PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	sodium cacodylate	50 (mM)	pH6.5
10	1	reservoir	ammonium sulfate	0.2 (M)
11	1	reservoir	PEG8000	18 (%)
2	1	drop	HEPES	5 (mM)	pH7.5
3	1	drop	ammonium sulfate	0.1 (M)
4	1	drop	PEG8000	9 (%)
5	1	drop		0.25 (M)
6	1	drop	beta-mercaptoethanol	1 (mM)
7	1	drop	S-adenosyl-L-homocysteine	0.3 (mM)
8	1	drop	protein	10 (mg/ml)
9	1	reservoir	sodium cacodylate	0.1 (M)	pH6.5