5J49

Crystal structure of UDP-glucose pyrophosporylase / UTP-glucose-1-phosphate uridylyltransferase from Burkholderia xenovorans

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	2016-03-03
Detector	RAYONIX MX-225
Wavelength(s)	0.97872
Spacegroup name	P 41 21 2
Unit cell lengths	134.110, 134.110, 73.150
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.800
R-factor	0.1717
Rwork	0.171
R-free	0.20710
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3juj
RMSD bond length	0.007
RMSD bond angle	0.862
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.850
High resolution limit [Å]	1.800	8.050	1.800
Rmerge	0.051	0.020	0.530
Number of reflections	62217
<I/σ(I)>	33.26	89.54	5.27
Completeness [%]	100.0	97.6	100
Redundancy	12.2
CC(1/2)	1.000

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	290	Microlytic MCSG1 screen H7: 2M Ammonium sulphate, 100mM BisTris pH 5.5; BuxeA.00118.c.B1.PS02592 at 16mg/ml; cryo: 25% EG in two steps; tray 269868 h7, puck RPA3-4