9BH3

Structure of apo Aggregatibacter actinomycetemcomitans SiaP protein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron site	Australian Synchrotron
Beamline	MX2
Temperature [K]	110
Detector technology	PIXEL
Collection date	2019-05-05
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.91840
Spacegroup name	C 1 2 1
Unit cell lengths	138.667, 141.394, 109.405
Unit cell angles	90.00, 112.49, 90.00

Refinement procedure

Resolution	48.640 - 2.580
R-factor	0.19069
Rwork	0.189
R-free	0.21965
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.016
RMSD bond angle	1.530
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.20)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.640	2.650
High resolution limit [Å]	2.580	2.580
Number of reflections	61226	2476
<I/σ(I)>	6.3	1.6
Completeness [%]	100.0
Redundancy	3.6
CC(1/2)	0.995	0.783

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		292	Drops consisting of 400 nL of mother-liquor and protein solution (AaSiaP at 20 mg/mL along with and without 0.75 mM Neu5Ac in SEC buffer) were mixed using the Mosquito Protein Crystallization System and the sitting-drop vapor-diffusion method and incubated at 20 C. Apo AaSiaP crystals that grew in SG1 conditions C11 (0.2 M sodium acetate trihydrate, 0.1 M sodium cacodylate, pH 6.5, 30% (w/v) PEG 8000)