5EJE

Crystal structure of E. coli Adenylate kinase G56C/T163C double mutant in complex with Ap5a

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I911-2
Synchrotron site	MAX II
Beamline	I911-2
Temperature [K]	100
Detector technology	CCD
Collection date	2015-09-19
Detector	MAR CCD 165 mm
Wavelength(s)	1.038
Spacegroup name	P 21 2 21
Unit cell lengths	73.003, 79.064, 81.834
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.800 - 1.900
R-factor	0.1889
Rwork	0.186
R-free	0.23580
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ake
RMSD bond length	0.003
RMSD bond angle	0.756
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.10_2140: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	26.800	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.120	1.990
Number of reflections	37833
<I/σ(I)>	18.8	1.8
Completeness [%]	99.6	97.5
Redundancy	14.6	14.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.8	291	Purified AdK in 50 mM NaCl and 30 mM MES buffer, pH 6.0 was concentrated to 13 mg/ml and co-crystallized with a 5 molar excess of Ap5a. A typical drop contained 1 microL of protein mixed with 1 microL of precipitant and equilibrated against 1 mL reservoir solution containing 26-28% PEG 8K, 10 mM CoCl2 and 0.1 M NaOAc, pH 5.8).