3NEH

Crystal structure of the protein LMO2462 from Listeria monocytogenes complexed with ZN and phosphonate mimic of dipeptide L-Leu-D-Ala

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	100
Detector technology	CCD
Collection date	2010-03-04
Detector	ADSC QUANTUM 4
Wavelength(s)	0.97915
Spacegroup name	P 21 21 21
Unit cell lengths	53.834, 79.453, 152.014
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.727 - 1.642
R-factor	0.1979
Rwork	0.197
R-free	0.21930
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3lu2
RMSD bond length	0.007
RMSD bond angle	1.073
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	BALBES
Refinement software	PHENIX ((phenix.refine: 1.5_2))

Data quality characteristics

	Overall
Low resolution limit [Å]	39.727
High resolution limit [Å]	1.642
Rmerge	0.094
Number of reflections	75524
Completeness [%]	94.0

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	25% PEG 3350, 0.1M Bis-Tris, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K