2WBC

REFINED CRYSTAL STRUCTURE (2.3 ANGSTROM) OF A WINGED BEAN CHYMOTRYPSIN INHIBITOR AND LOCATION OF ITS SECOND REACTIVE SITE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU FR-D
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1996-05
Detector	RIGAKU
Spacegroup name	P 61 2 2
Unit cell lengths	61.800, 61.800, 212.810
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 2.300
R-factor	0.187
Rwork	0.187
R-free	0.24100
RMSD bond length	0.011
RMSD bond angle	27.192 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall
Low resolution limit [Å]	12.000
High resolution limit [Å]	2.300
Rmerge	0.095
Total number of observations	10551 *
Number of reflections	9897
Completeness [%]	80.1
Redundancy	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.4	4 *	PROTEIN WAS CRYSTALLIZED BY HANGING DROP VAPOUR DIFFUSION FROM 25% AMM. SULPHATE IN TRIS-HCL, 10MM NA ACETATE,400 MM NACL AT PH 5.4 AGAINST 25% AMM. SULPHATE,60MM NA ACETATE AT 4 DEGREE CENTIGRADE., vapor diffusion - hanging drop, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8.6 (mg/ml)
2	1	drop	Tris-HCl	71.4 (mM)
3	1	drop		286 (mM)
4	1	drop	ammonium sulfate	1.4 (%)
5	1	drop	sodium acetate	2.9 (mM)
6	1	reservoir	ammonium sulfate	25 (%)
7	1	reservoir	sodium acetate	60 (mM)