1OEW

ATOMIC RESOLUTION STRUCTURE OF NATIVE ENDOTHIAPEPSIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-06-15
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	42.720, 74.660, 42.550
Unit cell angles	90.00, 97.27, 90.00

Refinement procedure

Resolution	42.300 * - 0.910 *
R-factor	0.121
R-free	0.14700
Structure solution method	OTHER
RMSD bond length	0.015
RMSD bond angle	0.029
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SHELXL-97
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	42.300	0.960
High resolution limit [Å]	0.910	0.910
Rmerge	0.109	0.503
Number of reflections	186749
<I/σ(I)>	8.6	3
Completeness [%]	99.4	99.4
Redundancy	4.7	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Batch method *	4.6		BATCH METHOD WITH ENZYME AT A CONCENTRATION OF 2 MG/ML IN 100 MM SODIUM ACETATE BUFFER AT PH 4.6 (MOEWS AND BUNN, 1970) CRYSTALS LEFT TO GROW FOLLOWING SLOW ADDITION OF AMMONIUM SULPHATE TO FINAL CONCENTRATION OF 0.35 G/ML (55% SATURATION).

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	2 (mg/ml)
2	1	1	sodium acetate	100 (mM)	pH4.6
3	1	1	ammonium sulfate	55 (%sat)