9BHF

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	P 1 21 1
Unit cell lengths	66.166, 49.540, 121.389
Unit cell angles	90.00, 92.81, 90.00

Refinement procedure

Resolution	45.810 - 1.900
R-factor	0.2015
Rwork	0.200
R-free	0.23170
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	1.416
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.860	2.000
High resolution limit [Å]	1.900	1.900
Number of reflections	62386	6175
<I/σ(I)>	6.2
Completeness [%]	99.8
Redundancy	2
CC(1/2)	0.995	0.505

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	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. Neu5Ac (0.75 mM) bound AaSiaP crystals including grew in SG1 condition H2 (30% w/v PEG 4000) were not cryo-protected before being flash-cooled in liquid nitrogen prior to data collection