3LBF

Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007
Temperature [K]	100
Collection date	2009-10-28
Wavelength(s)	1.00
Spacegroup name	P 1
Unit cell lengths	52.300, 55.060, 67.490
Unit cell angles	74.00, 74.70, 85.57

Refinement procedure

Resolution	25.000 - 1.800
R-factor	0.2151
Rwork	0.213
R-free	0.24720
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2yxe
RMSD bond length	0.012
RMSD bond angle	1.240
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.056	0.207
Number of reflections	62259
<I/σ(I)>	10.7	3.9
Completeness [%]	96.2
Redundancy	2.8	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	288	Hepes-Na, monosodium dihydrogen phosphate, monopotassium dihydrogen phosphate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 288K