3EIB

Crystal structure of K270N variant of LL-diaminopimelate aminotransferase from Arabidopsis thaliana

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	100
Detector technology	CCD
Collection date	2008-02-09
Detector	ADSC QUANTUM 315
Wavelength(s)	0.976067
Spacegroup name	P 32 2 1
Unit cell lengths	103.045, 103.045, 171.984
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	39.590 - 1.850
R-factor	0.16401
Rwork	0.162
R-free	0.19749
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2z20
RMSD bond length	0.015
RMSD bond angle	1.344
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	1.920
High resolution limit [Å]	1.850	1.850
Number of reflections	83053
Completeness [%]	91.4	89.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	45% (NH4)2SO4, 0.1 M HEPES pH 7.5, 3% PEG400, VAPOR DIFFUSION, HANGING DROP, temperature 298K