4F3P

Crystal structure of a Glutamine-binding periplasmic protein from Burkholderia pseudomallei in complex with glutamine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	100
Detector technology	CCD
Collection date	2012-04-01
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9774
Spacegroup name	P 1 21 1
Unit cell lengths	56.330, 74.500, 60.190
Unit cell angles	90.00, 100.63, 90.00

Refinement procedure

Resolution	50.000 - 2.400
R-factor	0.1789
Rwork	0.177
R-free	0.21520
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ggg modified with CCP4 program chainsaw
RMSD bond length	0.014
RMSD bond angle	1.588
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.3.0)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.460
High resolution limit [Å]	2.400	10.730	2.400
Rmerge	0.086	0.020	0.524
Number of reflections	19249	230	1394
<I/σ(I)>	14.36	48.8	2.6
Completeness [%]	99.9	98.3	99.6
Redundancy	3.8	3.6	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	MD Morpheus screen C12: 12.5% PEG 3350, 12.5% PEG 1000, 12.5% MPD, 30mM sodium nitrate, 30mM disodium hydrgon phosphate, 30mM ammonium sulphate, 100mM bicine/trizma; BupsA.17285.b.A2 PW PS01148 20mg/ml, tray 232242c12, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 290K