9AV8

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	2020-12-03
Detector	DECTRIS EIGER X 16M
Wavelength(s)	1.0
Spacegroup name	P 21 21 2
Unit cell lengths	77.680, 185.240, 64.450
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.290 - 2.592
R-factor	0.253
Rwork	0.250
R-free	0.30650
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.007
RMSD bond angle	0.890
Data reduction software	autoPROC
Data scaling software	autoPROC
Phasing software	BUSTER
Refinement software	BUSTER (2.11.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	185.240	2.952
High resolution limit [Å]	2.592	2.592
Rmerge	0.196	0.957
Rpim	0.083	0.410
Number of reflections	12730	637
<I/σ(I)>	7.3	2
Completeness [%]	92.1	66.6
Redundancy	6.6	6.3
CC(1/2)	0.996	0.546

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.