7P76

Re-engineered 2-deoxy-D-ribose-5-phosphate aldolase catalysing asymmetric Michael addition reactions, Schiff base complex with cinnamaldehyde

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-1
Synchrotron site	ESRF
Beamline	MASSIF-1
Temperature [K]	100
Detector technology	CCD
Collection date	2021-06-06
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9655
Spacegroup name	P 1
Unit cell lengths	80.270, 92.788, 106.894
Unit cell angles	88.96, 88.83, 89.08

Refinement procedure

Resolution	80.240 - 1.900
R-factor	0.2378
Rwork	0.235
R-free	0.28290
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7p75
Data reduction software	XDS (20210205)
Data scaling software	Aimless (0.7.7)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.19.2)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	80.240	80.240	1.930
High resolution limit [Å]	1.900	10.410	1.900
Rmerge	0.112	0.042	0.587
Rmeas	0.158	0.060	0.830
Rpim	0.112	0.042	0.587
Total number of observations	374113	2500	18962
Number of reflections	229190	1385	11296
<I/σ(I)>	2.5	4.6	1.3
Completeness [%]	94.3	93.7	93.8
Redundancy	1.6	1.8	1.7
CC(1/2)	0.980	0.995	0.719

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	291	Protein was concentrated to 16 mg/ml in 10 mM potassium phosphate. Crystals grew from hanging-drop vapour diffusion experiments using 13% PEG 3350, 10% isopropanol and 0.1 M HEPES pH 7.5 as reservoir solution