1IZD

Crystal structure of Aspergillus oryzae Aspartic Proteinase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-05-13
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	49.361, 79.421, 93.563
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	38.300 * - 1.900
R-factor	0.177
Rwork	0.177
R-free	0.21300
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	26.200 *
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	38.300	2.020
High resolution limit [Å]	1.900	1.900
Rmerge	0.051	0.123 *
Total number of observations	74057 *
Number of reflections	27237 *
Completeness [%]	91.7	86.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	5	298	PEG4200, ammonium acetate sodium acetate trihydrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	reservoir	PEG4000	30 (%(w/v))
3	1	reservoir	ammonium acetate	200 (mM)
4	1	reservoir	sodium acetate trihydrate	100 (mM)	pH5.0