3FWW

The crystal structure of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase from Yersinia pestis CO92

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2008-10-06
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9794
Spacegroup name	P 63 2 2
Unit cell lengths	88.318, 88.318, 251.931
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	34.804 - 2.500
R-factor	0.2173
Rwork	0.214
R-free	0.27660
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hv9
RMSD bond length	0.007
RMSD bond angle	1.078
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	MERLOT
Refinement software	PHENIX ((phenix.refine))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.804	2.540
High resolution limit [Å]	2.500	2.500
Rmerge	0.079	0.713
Number of reflections	20468
<I/σ(I)>	31.96	1.58
Completeness [%]	96.2	87.7
Redundancy	9.4	5.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	289	0.17M Sodium Acetate, Tris-HCl, 25.5% PEG4000, 15% Glycerol, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K