6ANS

Crystal structure of a putative uncharacterized protein from Burkholderia cenocepacia

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	2017-06-23
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	62.100, 134.470, 98.080
Unit cell angles	90.00, 90.43, 90.00

Refinement procedure

Resolution	46.071 - 2.200
R-factor	0.1513
Rwork	0.150
R-free	0.18840
Structure solution method	SAD
RMSD bond length	0.008
RMSD bond angle	0.911
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.7.17)
Refinement software	PHENIX (dev_2849)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	46.071	50.000	2.260
High resolution limit [Å]	2.200	9.840	2.200
Rmerge	0.085	0.027	0.528
Rmeas	0.099	0.032	0.612
Number of reflections	81463	1737	11897
<I/σ(I)>	12.6	32.06	2.84
Completeness [%]	99.8	97.2	99.9
Redundancy	3.863	3.596	3.882
CC(1/2)	0.997	0.998	0.879

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	289	Microlytic MCSG 1 screen, B1 (100 mM MES/sodium hydroxide, pH 6.5, 20% w/v PEG4000, 0.6 M sodium chloride), 20 mg/mL BuceA.18021.a.A1.PD00490 (SE-MET), cryoprotectant: 20% ethylene glycol, tray 290946 B1, puck QUF9-5