7N09

Structural basis for branched substrate selectivity in a ketoreductase from Ascaris suum

Replaces:  6U5I

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.3.1
Synchrotron site	ALS
Beamline	8.3.1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-05-05
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	0.73
Spacegroup name	C 1 2 1
Unit cell lengths	128.542, 54.942, 89.270
Unit cell angles	90.00, 131.04, 90.00

Refinement procedure

Resolution	67.330 - 2.000
R-factor	0.1789
Rwork	0.177
R-free	0.22000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1e6w
RMSD bond length	0.016
RMSD bond angle	1.105
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	BALBES
Refinement software	PHENIX (1.14_3260)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	67.330	1.810
High resolution limit [Å]	1.750	1.750
Number of reflections	84379	4507
<I/σ(I)>	12.5
Completeness [%]	89.4
Redundancy	2
CC(1/2)	0.999	0.196

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION	6.5	290	35% PEG550 MME, 144 mM potassium sodium tartrate, 100 mM MES, pH6.5 2 M sodium malonate, pH 6.5
1	EVAPORATION	6.5	290	35% PEG550 MME, 144 mM potassium sodium tartrate, 100 mM MES, pH6.5 2 M sodium malonate, pH 6.5