3BTK

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	75.370, 84.570, 122.810
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.850
Rwork	0.202
R-free	0.23000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2ptc
RMSD bond length	0.010
RMSD bond angle	1.870
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	1.950
High resolution limit [Å]	1.850	1.850
Rmerge	0.069	0.329
Number of reflections	33755
<I/σ(I)>	7.4	2.2
Completeness [%]	99.1	100
Redundancy	4	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5	37 *	pH 7.5

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)