1IBQ

ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200H
Temperature [K]	290
Detector technology	AREA DETECTOR
Collection date	1999-01-01
Detector	ENRAF-NONIUS FAST
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	82.190, 36.620, 104.940
Unit cell angles	90.00, 113.49, 90.00

Refinement procedure

Resolution	26.340 - 2.140
R-factor	0.21
Rwork	0.221
R-free	0.26900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	1.200
Data reduction software	MADNESS
Data scaling software	SCALA
Phasing software	SHELX
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	26.340	2.270
High resolution limit [Å]	2.140	2.140
Rmerge	0.068	0.120
Total number of observations	88563 *
Number of reflections	26402
<I/σ(I)>	11.4
Completeness [%]	86.6 *	43.7 *
Redundancy	3.3	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	277	18% PEG8000, 0.1M sodium cacodylate, 0.2M zinc acetate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	PEG8000	18 (%)
3	1	reservoir	sodium cacodylate	0.1 (M)
4	1	reservoir	zinc acetate	200 (mM)