2Z20

Crystal structure of LL-Diaminopimelate Aminotransferase from Arabidopsis thaliana

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-2
Synchrotron site	SSRL
Beamline	BL9-2
Temperature [K]	100
Detector technology	CCD
Collection date	2006-11-26
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9793, 0.9795, 0.9185
Spacegroup name	P 32 2 1
Unit cell lengths	102.909, 102.909, 171.452
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 1.950
R-factor	0.18387
Rwork	0.182
R-free	0.22713
Structure solution method	MAD
RMSD bond length	0.017
RMSD bond angle	1.679
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	SHARP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.020
High resolution limit [Å]	1.950	1.950
Number of reflections	72271
<I/σ(I)>	15.4	2.3
Completeness [%]	93.6	94.4
Redundancy	6.2	5.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	45% (NH4)2SO4, 0.1M HEPES pH7.5, 3% PEG400, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K