1GL1

structure of the complex between bovine alpha-chymotrypsin and PMP-C, an inhibitor from the insect Locusta migratoria

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE DW32
Synchrotron site	LURE
Beamline	DW32
Temperature [K]	300
Collection date	1997-11-15
Spacegroup name	P 65
Unit cell lengths	92.958, 92.958, 165.841
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	19.660 - 2.100
R-factor	0.189
Rwork	0.189
R-free	0.22800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1cho
RMSD bond length	0.006
RMSD bond angle	1.310 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000 *	2.200
High resolution limit [Å]	2.100	2.100
Rmerge	0.079	0.371
Number of reflections	46359
Completeness [%]	98.2	89.6
Redundancy	3.9	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5	20 *	0.1 M NA ACETATE PH 5, 29% PEG 400, 0.1 M CDCL2

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	sodium acetate	100 (mM)
2	1	reservoir	PEG400	29 (%)
3	1	reservoir		100 (mM)	pH5.0
4	1	drop	protein	10 (mg/ml)