4QHQ

The structure of a nutrient binding protein from Burkholderia cenocepacia bound to methionine

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	2014-04-03
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97857
Spacegroup name	P 1 21 1
Unit cell lengths	31.630, 67.170, 55.480
Unit cell angles	90.00, 101.60, 90.00

Refinement procedure

Resolution	28.570 - 1.400
R-factor	0.1683
Rwork	0.167
R-free	0.19480
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3tqw
RMSD bond length	0.005
RMSD bond angle	1.093
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.5.5)
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	28.570		1.440
High resolution limit [Å]	1.400	6.260	1.400
Rmerge	0.042	0.021	0.275
Number of reflections	43114	395	3064
<I/σ(I)>	19.66	34.81	5.13
Completeness [%]	96.3	75.5	92.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	298	20mg/ml BuceA.18560.a.B1.PS01924, 100mM succinic acid, 15% PEG3350, 20% Ethylene glycol as a cryoprotectant, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 298K