9C35

Proline utilization A with the covalent acyl-enzyme intermediate in the aldehyde dehydrogenase active site

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-C
Synchrotron site	APS
Beamline	24-ID-C
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-11-10
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97918
Spacegroup name	P 1 21 1
Unit cell lengths	101.779, 103.119, 127.918
Unit cell angles	90.00, 106.51, 90.00

Refinement procedure

Resolution	97.580 - 1.740
R-factor	0.2125
Rwork	0.211
R-free	0.24910
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.010
RMSD bond angle	1.105
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHENIX
Refinement software	PHENIX ((1.20.1_4487: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	103.120	1.770
High resolution limit [Å]	1.740	1.740
Rmerge	0.161	1.665
Rmeas	0.187	1.983
Rpim	0.094	1.052
Total number of observations		23395
Number of reflections	468186	7749
<I/σ(I)>	4.5	0.3
Completeness [%]	96.2
Redundancy	3.8	3
CC(1/2)	0.986	0.331

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		286	CRYSTALLIZATION: 5 mg/mL PROTEIN, 20% (W/V) PEG-3350, 0.15M AMMONIUM SULFATE, 0.1M MGCL2, 0.1M HEPES AT PH 8.0, 0.1M NA FORMATE, 10 mM NAD+. CRYSTAL WAS SOAKED IN 20% (W/V) PEG-200, 40 mM L-PROLINE, 1 mM COENZYME Q1, 1mM NAD+, FOR 24 HRS AND THEN FLASH-COOLED IN LIQUID NITROGEN