6MVU

Structure of a bacterial ALDH16 active site mutant C295A complexed with p-nitrophenylacetate

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	2017-11-02
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	0.9791
Spacegroup name	P 21 21 21
Unit cell lengths	79.383, 119.623, 158.670
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	95.519 - 1.488
R-factor	0.1928
Rwork	0.192
R-free	0.21580
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	homology model built with Swiss-Model using 5kf6 as the template
Data reduction software	XDS
Data scaling software	Aimless (0.5.23)
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	119.620	1.510
High resolution limit [Å]	1.488	1.488
Rmerge	0.133	1.799
Rmeas	0.144	1.952
Rpim	0.055	0.748
Number of reflections	470410	11001
<I/σ(I)>	8.8
Completeness [%]	98.8	90.8
Redundancy	6.7	6.5
CC(1/2)	0.998	0.440

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	293	Protein was concentrated to 6 mg/ml in a storage buffer consisting of 20 mM Tris-HCl at pH 8.0, 100 mM NaCl, 2.5% glycerol and 0.5 mM TCEP. The crystallization reservoir solution contained 20% (w/v) polyethylene glycol (PEG) 3350, 200 mM ammonium sulfate and 100 mM Bis-Tris at pH 5.5.