5KHA

Structure of glutamine-dependent NAD+ synthetase from Acinetobacter baumannii in complex with adenosine diphosphate (ADP)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2016-05-25
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	71.880, 123.750, 73.650
Unit cell angles	90.00, 110.93, 90.00

Refinement procedure

Resolution	41.242 - 2.100
R-factor	0.1663
Rwork	0.165
R-free	0.21030
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4f4h
RMSD bond length	0.007
RMSD bond angle	0.898
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX (dev_2429)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.150
High resolution limit [Å]	2.100	9.390	2.100
Rmerge	0.099	0.023	0.540
Number of reflections	69741
<I/σ(I)>	10.83	44.1	2.58
Completeness [%]	99.3	95.7	98
Redundancy	3.7
CC(1/2)	0.996

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	Microlytic MCSG1, condition H5: 20% PEG 3350, 200mM KCl; AcbaC.18002.a.B1.PS02475 at 19.5mg/ml with 2mM of each AMPPNP, Glutamate, MgCl2, PPi; cryo: 20% EG with 2mM NAD/Mg; puck: exo0-1, tray: 266048 h5