3SLG

Crystal structure of PbgP3 protein from Burkholderia pseudomallei

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	2011-04-23
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97740
Spacegroup name	P 1 21 1
Unit cell lengths	83.570, 91.550, 147.260
Unit cell angles	90.00, 91.63, 90.00

Refinement procedure

Resolution	50.000 - 2.100
R-factor	0.1793
Rwork	0.177
R-free	0.22130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1z7e
RMSD bond length	0.015
RMSD bond angle	1.307
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.1.4)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.150
High resolution limit [Å]	2.100	9.390	2.100
Rmerge	0.060	0.013	0.428
Number of reflections	128239	1483	9461
<I/σ(I)>	14.24	53.95	2.23
Completeness [%]	99.0	96.7	99.4
Redundancy	2.8		2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	289	protein at 8.2 mg/mL against PACT screen condition C10, 20% PEG 6000, 0.2 M MgCl2, 0.1 M Hepes, 20% ethylene glycol as cryo-protection reagent, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K