1TLD

CRYSTAL STRUCTURE OF BOVINE BETA-TRYPSIN AT 1.5 ANGSTROMS RESOLUTION IN A CRYSTAL FORM WITH LOW MOLECULAR PACKING DENSITY. ACTIVE SITE GEOMETRY, ION PAIRS AND SOLVENT STRUCTURE

Experimental procedure

Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X31
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X31
Detector technology	FILM
Wavelength(s)	1.009
Spacegroup name	P 21 21 21
Unit cell lengths	63.700, 63.500, 68.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	7.000 - 1.500
Rwork	0.167
RMSD bond length	0.015
RMSD bond angle	2.170
Data reduction software	FILME
Data scaling software	PROTEIN
Phasing software	PROTEIN
Refinement software	EREF

Data quality characteristics

	Overall
High resolution limit [Å]	1.500 *
Rmerge	0.046 *
Total number of observations	58592 *
Number of reflections	28553 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6 *	22 *	THE SOLVENT USED WAS 2.5 M AMMONIUM SULPHATE, 0.1 M PHOSPHATE, 1 MM CACL AT PH 5.3.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	ammonium sulfate
3	1	reservoir		1 (mM)
4	1	reservoir	benzamidine	20 (mg/ml)