9C36

Proline utilization A complexed with the substrate L-glutamate gamma-semialdehyde 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	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Temperature [K]	100
Detector technology	CMOS
Collection date	2022-04-29
Detector	RDI CMOS_8M
Wavelength(s)	1.07216
Spacegroup name	P 1 21 1
Unit cell lengths	100.870, 101.820, 126.030
Unit cell angles	90.00, 106.53, 90.00

Refinement procedure

Resolution	48.350 - 1.470
R-factor	0.1815
Rwork	0.180
R-free	0.20680
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.009
RMSD bond angle	1.072
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]	48.350	1.500
High resolution limit [Å]	1.470	1.470
Rmerge	0.069	0.910
Rmeas	0.076	1.171
Rpim	0.031	0.723
Total number of observations		37151
Number of reflections	751867	16019
<I/σ(I)>	12.6	0.8
Completeness [%]	97.7
Redundancy	4.9	2.3
CC(1/2)	0.998	0.357

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		286	CRYSTALLIZATION: 5 mg/mL PROTEIN, 14% (W/V) PEG-3350, 0.2M AMMONIUM SULFATE, 0.1M MGCL2, 0.1M HEPES AT PH 8.0, 0.1M NA FORMATE, 10 mM NAD+. CRYTAL WAS SOAKED IN 20% (W/V) PEG-200, 40 mM L-PROLINE, 1 mM COENZYME Q1, 1mM NAD+ for 1 MIN AND THEN FLASH-COOLED IN LIQUID NITROGEN