3BTF

THE CRYSTAL STRUCTURES OF THE COMPLEXES BETWEEN BOVINE BETA-TRYPSIN AND TEN P1 VARIANTS OF BPTI.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM1A
Synchrotron site	ESRF
Beamline	BM1A
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1998-04
Detector	MARRESEARCH
Spacegroup name	I 2 2 2
Unit cell lengths	75.630, 85.230, 122.870
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.800
Rwork	0.194
R-free	0.22500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2ptc
RMSD bond length	0.008
RMSD bond angle	1.460
Data reduction software	DENZO
Data scaling software	CCP4
Phasing software	X-PLOR
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.059	0.326
Number of reflections	36655
<I/σ(I)>	8.4	2.2
Completeness [%]	98.1	98.8
Redundancy	4	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5	37 *	0.1 M HEPES PH 7.5 48% AMMONIUM SULPHATE

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	27 (mg/ml)
2	1	reservoir	ammonium sulfate	48-50 (%sat)
3	1	reservoir	HEPES	0.1 (M)