4ZJU

Structure of a NADH-dependent enoyl-ACP reductase from Acinetobacter baumannii in complex with NAD

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2015-04-09
Detector	RAYONIX MX-300
Wavelength(s)	0.97856
Spacegroup name	I 2 2 2
Unit cell lengths	71.020, 92.440, 93.830
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.915 - 1.200
R-factor	0.1252
Rwork	0.125
R-free	0.14200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4nqz
RMSD bond length	0.006
RMSD bond angle	1.269
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	5.370	1.230
High resolution limit [Å]	1.200	3.790	1.200
Rmerge	0.049	0.017	0.537
Rmeas	0.055	0.020	0.607
Total number of observations	463957
Number of reflections	96282	2064	7053
<I/σ(I)>	18.71	62.76	2.75
Completeness [%]	99.9	100	100
Redundancy	4.8		4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	290	Molecular Dimensions Morpheus screen, h12: Morpheus H12: 20mM each L-Na-Glutamate, Alanine (racemic), Glycine, Lysine HCl (racemic), Serine (racemic); 100mM Tris (base)/Bicine pH 8.5; 15% each MPD (racemic), PEG 1000, PEG 3350; AcbaC.00170.a.B1.PW37673 at 25mg/ml with 5mM NADH; tray 262582, puck oxi7-1