1R74

Crystal Structure of Human Glycine N-Methyltransferase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR591
Temperature [K]	103
Detector technology	IMAGE PLATE
Collection date	2002-04-02
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 21 21 2
Unit cell lengths	75.840, 83.230, 114.880
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	12.000 - 2.550
R-factor	0.22492
Rwork	0.222
R-free	0.26605
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1xva
RMSD bond length	0.027
RMSD bond angle	2.167
Data scaling software	CCP4 ((SCALA))
Phasing software	CNS
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	12.000	2.690
High resolution limit [Å]	2.550	2.550
Number of reflections	23864
<I/σ(I)>	9.9	1.8
Completeness [%]	98.3	98.3
Redundancy	3.7	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	273	PEG4000, Na citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 273K
1	VAPOR DIFFUSION, HANGING DROP	5.6	273	PEG4000, Na citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 273K