8U93

Crystal structure of N-acetylneuraminate lyase (NanA) from Klebsiella aerogenes (PEG bound)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 19-ID
Synchrotron site	NSLS-II
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-02-20
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9795
Spacegroup name	P 62 2 2
Unit cell lengths	96.406, 96.406, 205.982
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	36.940 - 1.900
R-factor	0.1842
Rwork	0.183
R-free	0.20200
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.093
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.21rc1_5057: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.200	1.940
High resolution limit [Å]	1.900	1.900
Rmerge	0.075	3.276
Rmeas	0.076	3.315
Rpim	0.012	0.508
Total number of observations	1794646	118584
Number of reflections	45341	2859
<I/σ(I)>	30.8	1.9
Completeness [%]	99.8
Redundancy	39.6	41.5
CC(1/2)	1.000	0.914

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	Index E8: 35% v/v Pentaerythritol propoxylate (5/4 PO/OH), 0.05 M HEPES pH 7.5, 0.2 M Potassium chloride. KlaeA.01563.a.B1.PW39186 at 18.6 mg/mL. 2mM pyruvate added to the protein prior to crystallization. Plate 13192, well E8 drop 2. Puck: PSL-1406, Cryo: direct