1EUF

BOVINE DUODENASE(NEW SERINE PROTEASE), CRYSTAL STRUCTURE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	295
Detector technology	IMAGE PLATE
Collection date	1997-08-04
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 64
Unit cell lengths	100.117, 100.117, 39.753
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	99.000 - 2.400
Rwork	0.179
R-free	0.22300
RMSD bond length	0.006
RMSD bond angle	24.670 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	99.000	2.510
High resolution limit [Å]	2.400	2.400
Rmerge	0.058	0.247
Total number of observations	87183 *
Number of reflections	8780
<I/σ(I)>	14.3
Completeness [%]	96.3	97.3
Redundancy	9.7	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.7	4 *	Zamolodchikova, T.S., (1997) Eur. J. Biochem., 249, 612. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	PEG3350	10 (%)
3	1	drop	K/Na phosphate	50 (mM)
4	1	drop		1 (mM)
5	1	reservoir	PEG3350	14 (%sat)