9AV5

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	2020-02-28
Detector	DECTRIS EIGER X 16M
Wavelength(s)	1.0
Spacegroup name	C 1 2 1
Unit cell lengths	185.990, 77.040, 65.070
Unit cell angles	90.00, 90.58, 90.00

Refinement procedure

Resolution	32.530 - 2.363
R-factor	0.2206
Rwork	0.219
R-free	0.25850
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.900
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]	92.990	2.727
High resolution limit [Å]	2.363	2.363
Rmerge	0.101	0.659
Rpim	0.065	0.451
Number of reflections	19492	975
<I/σ(I)>	9.4
Completeness [%]	87.5	57.9
Redundancy	3.4	2.9
CC(1/2)	0.990	0.584

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	protein was incubated at 12 mg/ml with 1 mM NAD+ and 1 mM compound 1 with the addition of 0.125% B-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.