7K47

Crystal Structure of Glucosamine-1-phosphate N-acetyltransferase from Stenotrophomonas maltophilia K279a

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	2020-07-16
Detector	RAYONIX MX-300
Wavelength(s)	0.97856
Spacegroup name	P 63
Unit cell lengths	91.290, 91.290, 184.550
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.880 - 2.900
R-factor	0.1774
Rwork	0.174
R-free	0.20540
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	two domains of PDB entry 5vmk as per Morda
RMSD bond length	0.004
RMSD bond angle	0.610
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MoRDa
Refinement software	PHENIX (1.18.2)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.980
High resolution limit [Å]	2.900	12.970	2.900
Rmerge	0.051	0.037	0.543
Rmeas	0.054	0.040	0.568
Number of reflections	19333	223	1433
<I/σ(I)>	30.57	52.9	4.83
Completeness [%]	99.9	95.7	100
Redundancy	11.482	8.91	11.585
CC(1/2)	1.000	0.999	0.947

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	287	Optimization screen based on Rigaku Reagens JCSG+ condition B4: 100mM HEPES free acid / Sodium hydroxide pH 8.0, 8% (V/V) ethylene glycol, 9.6% (w/V) PEG 8000: StmaA.00150.a.B1.PW38698 at 24mg/ml: tray 319930h10: cryo: 20% EG in 2 steps: puck aod1-6