2Z1Z

Crystal structure of LL-Diaminopimelate Aminotransferase from Arabidopsis thaliana complexed with L-malate ion

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.3.1
Synchrotron site	ALS
Beamline	8.3.1
Temperature [K]	100
Detector technology	CCD
Collection date	2006-10-12
Detector	ADSC QUANTUM 210
Wavelength(s)	1.11590
Spacegroup name	P 32 2 1
Unit cell lengths	102.587, 102.587, 172.939
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.400
R-factor	0.18309
Rwork	0.180
R-free	0.25073
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Native LL-diaminopimelate aminotransferase structure
RMSD bond length	0.028
RMSD bond angle	2.374
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.490
High resolution limit [Å]	2.400	2.400
Number of reflections	37831
<I/σ(I)>	13.5	1.9
Completeness [%]	90.4	93.6
Redundancy	4	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	298	2.1M D,L-malic acid, pH7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K