1PJA

The crystal structure of palmitoyl protein thioesterase-2 reveals the basis for divergent substrate specificities of the two lysosomal thioesterases (PPT1 and PPT2)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE A1
Synchrotron site	CHESS
Beamline	A1
Detector technology	CCD
Detector	ADSC QUANTUM 4
Wavelength(s)	0.943
Spacegroup name	P 62 2 2
Unit cell lengths	148.520, 148.520, 152.510
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	40.000 - 2.700
R-factor	0.251
Rwork	0.221
R-free	0.24500 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.090 *
RMSD bond angle	1.300 *
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000
High resolution limit [Å]	2.700	2.700
Rmerge	0.046 *
Number of reflections	34721
<I/σ(I)>	15.7	2.5
Completeness [%]	100.0 *
Redundancy	6.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	6	4 *	1.8-2.2M ammonium sulfate, 8% methyl-pentane-diol, 100 mM MES , pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	reservoir	ammonium sulfate	2 (M)
3	1	reservoir	sodium cacodylate	100 (mM)	pH5.5-6.5
4	1	reservoir	MPD	8 (%)