4OAQ

Crystal structure of the R-specific Carbonyl Reductase from Candida parapsilosis ATCC 7330

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	93
Detector technology	IMAGE PLATE
Collection date	2012-09-19
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	65.724, 99.896, 116.662
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.974 - 1.858
R-factor	0.2038
Rwork	0.201
R-free	0.24950
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1piw
RMSD bond length	0.008
RMSD bond angle	1.225
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: 1.8_1069))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	24.974	1.930
High resolution limit [Å]	1.858	1.860
Rmerge	0.089	0.590
Number of reflections	62705
<I/σ(I)>	5.46	2.13
Completeness [%]	96.1	97.7
Redundancy	4.9	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	protein sample (13.5 mg/ml) was mixed with an equal volume of reservoir solution and equilibrated against the latter. The reservoir solution consisted of 25%(w/v) PEG 4000 as a precipitant, 0.1 M HEPES pH 7.5 as buffer, and 8% isopropanol and 0.1 mM ZnCl2 as additives., VAPOR DIFFUSION, HANGING DROP, temperature 293K