5TVK

Crystal Structure of putative plasmid partition protein (BB_S35) from Borrelia burgdorferi B31 bound to AMPPNP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2016-07-05
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 65
Unit cell lengths	57.320, 57.320, 343.570
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	28.269 - 2.400
R-factor	0.1729
Rwork	0.169
R-free	0.21800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3k9g
RMSD bond length	0.008
RMSD bond angle	0.899
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MoRDa
Refinement software	PHENIX (1.11.1_2575)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	49.600		2.360
High resolution limit [Å]	2.300	10.290	2.300
Rmerge	0.050	0.030	0.485
Number of reflections	76639
<I/σ(I)>	12.32	28.04	2.25
Completeness [%]	90.4	76.1	93
Redundancy	2.81
CC(1/2)	0.998	0.997	0.884

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	290	Morpheus F2: 10% w/v PEG8000, 20% v/v ethylene glycol, 0.2 M D-glucose, 0.2 M D-mannose, 0.2 M D-galactose, 0.2 M L-fucose, 0.2 M D-xylose, 0.2 M N-acetyl-D-glucosamine, 0.1 M MES/imidazole, pH 6.5, direct cryoprotection, BobuA.01478.a.A1 PS00305 at 20 mg/mL, Tray268926f2, puck llm2-10, supplemented with 3 mM AMPPNP, 3 mM magnesium chloride, NDPs (possibly co-purified with the protein, as suggested by electron density)