7OBM

Crystal structure of the human Prolyl Endopeptidase-Like protein short form (residues 90-727)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-B
Synchrotron site	APS
Beamline	23-ID-B
Temperature [K]	100
Detector technology	CCD
Collection date	2015-07-12
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.979420
Spacegroup name	I 2 2 2
Unit cell lengths	64.920, 150.880, 220.660
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.670 - 3.100
R-factor	0.2469
Rwork	0.245
R-free	0.28210
Structure solution method	SAD
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.19_4092)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.670	48.670	3.180
High resolution limit [Å]	3.100	13.860	3.100
Rmerge	0.094	0.026	1.295
Rmeas	0.109	0.030	1.504
Total number of observations	149099
Number of reflections	37971	416	2797
<I/σ(I)>	11.53	42.79	0.99
Completeness [%]	99.9	96.5	99.9
Redundancy	3.927	3.714	3.921
CC(1/2)	0.998	0.999	0.428

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	277	200 nL of protein and 200 nL of reservoir were combined in a MRC SD2 crystallization plate by a Mosquito crystallization robot. The reservoir solution consisted of 2M ammonium sulfate and 0.1 M NaHEPES buffer, pH 7.5. The protein solution was 9.1mg/ml Nd88 PREPL, 5 mM HEPES, pH 7.5, 50 mM NaCL, 0.3 mM TCEP. Crystals were observed after one year incubation in the cold room.