8Q2B

E. coli Adenylate Kinase variant D158A (AK D158A) showing significant changes to the stacking of catalytic arginine side chains

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-2
Synchrotron site	ESRF
Beamline	ID23-2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-05-02
Detector	DECTRIS PILATUS3 X 6M
Wavelength(s)	0.87293
Spacegroup name	P 1 21 1
Unit cell lengths	57.283, 77.974, 59.911
Unit cell angles	90.00, 93.61, 90.00

Refinement procedure

Resolution	40.080 - 1.760
R-factor	0.1832
Rwork	0.181
R-free	0.22440
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.013
RMSD bond angle	1.307
Data reduction software	XDS (Oct 15, 2015)
Data scaling software	Aimless (0.5.25)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.19.2_4158-000)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.450	1.820
High resolution limit [Å]	1.760	1.760
Rmerge	0.109	1.097
Rmeas	0.118	1.183
Rpim	0.045	0.440
Number of reflections	52176	5114
<I/σ(I)>	11.2	1.82
Completeness [%]	100.0
Redundancy	6.9	7.1
CC(1/2)	0.998	0.627

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	Crystallization: 2 ul of purified AK-D158A at 16.4 mg/ml, mixed with the non-hydrolysable inhibitor Ap5A at a final concentration of 5 mM and 2 ul of precipitant buffer containing 32% PEG 8K, 0.2 M AmSO4, 0.1 M Cacodylate at pH 6.5.