6R6A

Major aspartyl peptidase 1 from C. neoformans

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-X
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-04-16
Detector	DECTRIS PILATUS 300K
Wavelength(s)	1.54187
Spacegroup name	C 2 2 21
Unit cell lengths	97.360, 112.641, 91.031
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	73.660 - 1.800
R-factor	0.1785
Rwork	0.177
R-free	0.20700
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	6r61
RMSD bond length	0.012
RMSD bond angle	1.597
Data reduction software	XDS
Data scaling software	XSCALE
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	73.660	73.660	1.910
High resolution limit [Å]	1.800	5.370	1.800
Rmerge	0.087	0.035	0.565
Rmeas	0.101	0.040	0.771
Total number of observations	138736
Number of reflections	39317	1854	2229
<I/σ(I)>	11.68	33.46	0.99
Completeness [%]	84.3	98.3	29.8
Redundancy	3.529	4.185	1.252
CC(1/2)	0.997	0.999	0.590

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		291	protein (83 mg/mL) in 50 mM sodium acetate, pH 5.0, 100 mM sodium chloride with reservoir solution composed of 200 mM lithium sulfate, 45% (v/v) PEG-400, 100 mM sodium acetate pH 4.5.