9AV4

Design and application of synthetic 17B-HSD13 substrates to drug discovery, and to reveal preserved catalytic activity of protective human variants

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 17-ID
Synchrotron site	APS
Beamline	17-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-02-10
Detector	DECTRIS EIGER X 16M
Wavelength(s)	1.0
Spacegroup name	C 1 2 1
Unit cell lengths	186.970, 76.060, 65.240
Unit cell angles	90.00, 94.69, 90.00

Refinement procedure

Resolution	33.470 - 2.090
R-factor	0.2126
Rwork	0.211
R-free	0.23930
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	0.940
Data reduction software	autoPROC
Data scaling software	STARANISO
Phasing software	PHASER
Refinement software	BUSTER (2.11.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	93.170	2.360
High resolution limit [Å]	2.090	2.090
Rmerge	0.059	0.359
Rpim	0.038	0.330
Number of reflections	28362	1419
<I/σ(I)>	11.9	2
Completeness [%]	87.9	56.2
Redundancy	3.3	1.9
CC(1/2)	0.998	0.763

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	protein was incubated at 12 mg/ml with 1 mM NAD+ and 1 mM compound 1 with the addition of 0.125% beta-octyl-glucoside. Sitting drop vapor diffusion crystallization was set up by mixing 300 nl protein complex with 300 nl of reservoir solution containing 30% PEG3350, 0.2 M ammonium chloride. Crystals grew at room temperature over 2 weeks.