6WM5

Structure of a phosphatidylinositol-phosphate synthase (PIPS) from Mycobacterium kansasii

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-02-21
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.9791
Spacegroup name	P 1 21 1
Unit cell lengths	78.338, 60.241, 85.377
Unit cell angles	90.00, 90.91, 90.00

Refinement procedure

Resolution	49.220 - 1.961
R-factor	0.2369
Rwork	0.235
R-free	0.27700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5d91 4o6m
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]	49.220	2.037
High resolution limit [Å]	1.960	1.960
Rmerge	0.106	0.640
Rmeas	0.150	0.905
Rpim	0.106	0.640
Number of reflections	37482	183
<I/σ(I)>	6.23	0.98
Completeness [%]	66.0	3.27
Redundancy	1.9
CC(1/2)	0.989	0.110

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	LIPIDIC CUBIC PHASE	6	295	100 mM Sodium citrate, pH 6, 50 mM sodium chloride, 20 mM magnesium chloride hexahydrate, 22% PEG 400 (precipitant). Concentrated protein at 30-35 mg/ml was mixed with monoolein (Sigma) in a 1:1.5 protein to lipid ratio (w/w). Monoolein was doped with 2% CDP-DAG