5TPQ

E. coli alkaline phosphatase D101A, D153A, R166S, E322A, K328A mutant

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL12-2
Synchrotron site	SSRL
Beamline	BL12-2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-06-13
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.979
Spacegroup name	P 63 2 2
Unit cell lengths	160.720, 160.720, 138.360
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	38.600 - 2.450
R-factor	0.167
Rwork	0.165
R-free	0.21900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3tg0
RMSD bond length	0.010
RMSD bond angle	1.130
Data reduction software	XDS
Data scaling software	Aimless (0.5.25)
Phasing software	PHASER (2.6.1)
Refinement software	BUSTER (2.10.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	38.600	2.540
High resolution limit [Å]	2.450	2.450
Rmerge	0.594	5.600
Number of reflections	39204
<I/σ(I)>	7.8	1.2
Completeness [%]	99.5	95.6
Redundancy	35.5	30.4
CC(1/2)	0.995	0.318

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	298	5 mg/mL protein in 10 mM MOPS pH 7.0, 50 mM NaCl, 100 mM ZnCl2. Protein solution mixed with equal volume of precipitant solution: 23% PEG 3350, 0.2 M NH3F, 0.2 M HEPES pH=8.0