5VMK

Crystal structure of a bifunctional GlmU UDP-N-acetylglucosamine diphosphorylase/glucosamine-1- phosphate N-acetyltransferase from Acinetobacter baumannii

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2015-03-12
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 32 2 1
Unit cell lengths	96.620, 96.620, 262.420
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	47.512 - 2.550
R-factor	0.1872
Rwork	0.185
R-free	0.24850
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2oi6
RMSD bond length	0.007
RMSD bond angle	0.884
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX ((dev_2744: ???))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.512	47.512	2.620
High resolution limit [Å]	2.550	11.400	2.550
Rmerge	0.069	0.021	0.520
Rmeas	0.076	0.024	0.574
Number of reflections	47221	590	3446
<I/σ(I)>	17.89	47.02	3.62
Completeness [%]	99.7	91.6	99.9
Redundancy	5.535	4.466	5.64
CC(1/2)	0.999	1.000	0.910

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.2	289	AcbaC.00150.a.B1.PW37634 at 19.3 mg/mL against JCSG+ screen condition C6 40% PEG 300, 0.1 M phosphate-citrate pH 4.2, crystal tracking ID 261513c6, unique puck ID epp4-5