6WCT

Crystal structure of a guanylate kinase from Stenotrophomonas maltophilia K279a bound to guanosine-5'-monophosphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2020-03-19
Detector	RAYONIX MX300-HS
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	62.660, 101.420, 70.020
Unit cell angles	90.00, 92.03, 90.00

Refinement procedure

Resolution	47.510 - 2.100
R-factor	0.1822
Rwork	0.179
R-free	0.22940
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3tr0
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (phenix1.17.1-3660)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.510	47.510	2.150
High resolution limit [Å]	2.100	9.390	2.100
Rmerge	0.044	0.021	0.578
Rmeas	0.050	0.024	0.652
Total number of observations	237940
Number of reflections	51005	586	3760
<I/σ(I)>	18.97	54.46	2.98
Completeness [%]	99.9	97	100
Redundancy	4.665	4.292	4.688
CC(1/2)	0.999	0.999	0.903

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	287	33 mg/mL StmaA.01463.a.B1.PW38755 in 7 mM magnesium chloride, 7 mM ATP, 7 mM GMP (5GP) against MCSG1 screen condition B1 (0.6 M sodium chloride, 0.1 M MES, pH 6.5, 20% PEG4000), supplemented with 20% ethylene glycol as cryoprotectant, unique puck ID pfi1-7, crystal tracking ID 314557b1