5VE7

Crystal structure of UTP-glucose-1-phosphate uridylyltransferase from Burkholderia ambifaria in complex with UTP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2017-03-21
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	I 2 2 2
Unit cell lengths	63.250, 108.480, 124.510
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.092 - 2.300
R-factor	0.1817
Rwork	0.177
R-free	0.22130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	native structure 5vct
RMSD bond length	0.007
RMSD bond angle	0.892
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHENIX
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	39.092	2.360
High resolution limit [Å]	2.300	10.290	2.300
Rmerge	0.064	0.028	0.308
Rmeas	0.069	0.031	0.333
Number of reflections	19325	255	1341
<I/σ(I)>	20.79	40.3	7.51
Completeness [%]	99.3	97.3	94.2
Redundancy	7.055	6.071	7.159
CC(1/2)	0.999	0.999	0.984

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.07	290	Optimization screen around RigakuReagents JCSG B9: 100mM Sodium citrate / citric acid pH 5.07, 18.73% PEG 6000, BuamA.00118.a.B1.PS37963 at 45.5 mg/ml + 3mM GTP (BSI1746) + 3mM Glucose-1-phosphate (BSI 1952) + 3mM MgCl2, tray 289280h3: cryo: 25% EG in 3 steps: puck kzj0-7.