6S36

Crystal structure of E. coli Adenylate kinase R119K mutant

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-3
Synchrotron site	ESRF
Beamline	MASSIF-3
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-03-03
Detector	DECTRIS EIGER X 4M
Wavelength(s)	0.968
Spacegroup name	C 1 2 1
Unit cell lengths	135.690, 31.619, 53.171
Unit cell angles	90.00, 111.86, 90.00

Refinement procedure

Resolution	33.286 - 1.600
R-factor	0.1632
Rwork	0.159
R-free	0.23560
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4x8h
RMSD bond length	0.010
RMSD bond angle	0.992
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.13_2998: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.300	1.630
High resolution limit [Å]	1.600	1.600
Rmerge	0.056	0.665
Rpim	0.034	0.411
Number of reflections	27793	2806
<I/σ(I)>	16	2.4
Completeness [%]	99.1	99.9
Redundancy	6.8
CC(1/2)	0.998	0.775

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	291	Droplets of 2 to 4 microl protein solution in 30 mM MES pH 6.0 and 50 mM NaCl at 18 mg per ml and 5 molar excess of Ap5A were mixed with 2 microl reservoir solution consisting of 24-30% PEG 4000, 0.2 M MgCl2 and 100 mM Tris-HCl pH 8.5.