7P75

Re-engineered 2-deoxy-D-ribose-5-phosphate aldolase catalysing asymmetric Michael addition reactions in substrate-free state

This is a non-PDB format compatible entry.

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 21 1
Unit cell lengths	47.634, 67.497, 73.657
Unit cell angles	90.00, 101.05, 90.00

Refinement procedure

Resolution	47.000 - 1.230
Rwork	0.148
R-free	0.17140
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1p1x
RMSD bond length	0.007
RMSD bond angle	1.371
Data reduction software	XDS (20210205)
Data scaling software	Aimless (0.7.7)
Phasing software	PHASER (2.8.3)
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.000	47.000	1.250
High resolution limit [Å]	1.229	6.730	1.230
Rmerge	0.057	0.026	0.629
Rmeas	0.081	0.037	0.882
Rpim	0.057	0.026	0.617
Number of reflections	128757	816	5862
<I/σ(I)>	6.9
Completeness [%]	96.9	96.1
Redundancy	2.3	2.4	2.2
CC(1/2)	0.990	0.969	0.539

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.