1J71

Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	SIEMENS
Temperature [K]	293
Detector technology	AREA DETECTOR
Collection date	1994-06-27
Detector	SIEMENS-NICOLET X100
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	49.960, 51.430, 128.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 * - 1.800
R-factor	0.183 *
Rwork	0.165
R-free	0.22600 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1zap
RMSD bond length	0.011 *
RMSD bond angle	0.764 *
Data reduction software	SAINT
Data scaling software	SAINT
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall
Low resolution limit [Å]	30.000
High resolution limit [Å]	1.800
Rmerge	0.068 *
Total number of observations	215435 *
Number of reflections	32636 *
<I/σ(I)>	19
Completeness [%]	93.0
Redundancy	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	20 *	VAPOR DIFFUSION BY HANGING DROPS. 0.1 M SODIUM ACETATE, 20% ETHANOL, 1:1 WITH WATER SOLUTION OF THE PROTEIN (30 MG/ML)., pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	30 (mg/ml)
2	1	reservoir	sodium acetate	0.1 (M)
3	1	reservoir	ethanol	20 (%)