7APU

Structure of Adenylate kinase from Escherichia coli in complex with two ADP molecules refined at 1.36 A resolution.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2015-12-15
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97498
Spacegroup name	P 21 21 2
Unit cell lengths	72.754, 82.226, 78.783
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.810 - 1.360
R-factor	0.1854
Rwork	0.184
R-free	0.20600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ake
RMSD bond length	0.014
RMSD bond angle	1.564
Data reduction software	XDS
Data scaling software	Aimless (0.5.15)
Phasing software	PHASER
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	44.810	44.810	1.410
High resolution limit [Å]	1.360	5.270	1.360
Rmerge	0.062	0.032	1.017
Rmeas	0.067	0.035	1.094
Rpim	0.025	0.013	0.397
Number of reflections	99761	1922	9506
<I/σ(I)>	14.7		1.9
Completeness [%]	98.1	98.7	96
Redundancy	7.3	6.8	7.3
CC(1/2)	0.999	0.998	0.682

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	291.15	AdK at 18.3 mg/ml was mixed with 5 mM each of AMP and GTP in 30 mM MOPS buffer pH 7, containing 50 mM NaCl. Hanging drop: 2 ul of AdK, preincubated with AMP and GTP, and 2 ul of precipitant buffer containing 30% PEG 4000, 0.2 M NH4CH3CO2 (Ammonium Acetate), buffered with 100 mM CH3COONa (Sodium Acetate) adjusted to pH 4.6.