5UY7

Crystal structure of a peptidoglycan glycosyltransferase from Burkholderia ambifaria

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2017-02-15
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	C 2 2 21
Unit cell lengths	68.800, 74.310, 137.170
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.658 - 1.650
R-factor	0.1602
Rwork	0.159
R-free	0.18660
Structure solution method	SAD
RMSD bond length	0.005
RMSD bond angle	0.773
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.658	40.658	1.690
High resolution limit [Å]	1.650	7.380	1.650
Rmerge	0.059	0.046	0.461
Rmeas	0.064	0.050	0.495
Number of reflections	42618	526	3131
<I/σ(I)>	19.47	36.26	3.92
Completeness [%]	99.9	97.4	99.7
Redundancy	7.396	6.437	7.427
CC(1/2)	0.998	0.996	0.917

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	BuamA.10647.a.B2.PS37954 at 23.88 mg/mL against MCSG1 screen condition E5 0.1 M MES pH 6.5, 1.6 M MgSO4, crystal tracking ID 282706e5