9C34

Proline utilization A with the FADH- N5 atom covalently modified by proline

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-03-27
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97918
Spacegroup name	P 1 21 1
Unit cell lengths	101.603, 102.572, 127.203
Unit cell angles	90.00, 106.47, 90.00

Refinement procedure

Resolution	67.380 - 1.880
R-factor	0.1714
Rwork	0.170
R-free	0.20600
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.010
RMSD bond angle	1.060
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHENIX
Refinement software	PHENIX ((1.21_5207:0000))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	121.990	1.920
High resolution limit [Å]	1.880	1.880
Rmerge	0.103	1.173
Rmeas	0.111	1.273
Rpim	0.042	0.486
Total number of observations		56824
Number of reflections	385647	8769
<I/σ(I)>	12.5	1.4
Completeness [%]	97.2
Redundancy	7.1	6.5
CC(1/2)	0.998	0.534

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+. 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