5N2B

The crystal structure of Burkholderia pseudomallei antigen and type I fimbria protein BPSL1626.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Collection date	2016-02-05
Detector	MAR CCD 130 mm
Wavelength(s)	0.97
Spacegroup name	C 2 2 21
Unit cell lengths	91.866, 102.237, 72.435
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 - 1.900
R-factor	0.2107
Rwork	0.209
R-free	0.23730
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.002
RMSD bond angle	0.493
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	BALBES
Refinement software	PHENIX ((1.10.1_2155: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.000
High resolution limit [Å]	1.900	1.900
Rmerge	0.041
Rpim	0.016	0.188
Number of reflections	27236	3930
<I/σ(I)>	31.6	4.4
Completeness [%]	99.9	100
Redundancy	7.4	7.5
CC(1/2)	1.000	0.938

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	293	PACT Premier (Molecular Dimensions) condition I-9 (25% PEG 6000, 0.1M lithium chloride, 0.1M sodium acetate pH 5.0). Solution supplemented with 30% ethylene glycol as cryoprotectant.