1AB9

CRYSTAL STRUCTURE OF BOVINE GAMMA-CHYMOTRYPSIN

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	292
Detector technology	IMAGE PLATE
Collection date	1995-10-24
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 42 21 2
Unit cell lengths	69.520, 69.520, 97.810
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	5.000 - 1.600
R-factor	0.191
Rwork	0.191
R-free	0.19000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1gct
RMSD bond length	0.007
RMSD bond angle	26.600 *
Data reduction software	PROCESS
Data scaling software	PROCESS
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	69.500	1.650
High resolution limit [Å]	1.600	1.600
Rmerge	0.055	0.208
Total number of observations	332021 *
Number of reflections	31740
<I/σ(I)>	15.1	3.1
Completeness [%]	97.8	94.7
Redundancy	10.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	5.6		ALPHA-CHYMOTRYPSIN WAS DISSOLVED IN POTASSIUM BORATE (PH8.6) AND WAS INCUBATED AT 310K FOR 6 HOURS. SOLID AMMONIUM SULFATE WAS ADDED TO THE SOLUTION, AND THE PRECIPITATE FORMED WAS RECOVERED AND RE-DISSOLVED WITH WATER. CRYSTALLIZATION WAS DONE WITH A SITTING-DROP VAPOR-DIFFUSION PROCEDURE, IN WHICH PROTEIN SOLUTION (15MG/ML) CONTAINING 10MM CACODYLATE, 0.75% SATURATED ACETYLTRIMETHYL AMMONIUM AND 45% SATURATED AMMONIUM SULFATE WAS EQUILIBRATED AGAINST 65% SATURATED AMMONIUM SULFATE AT 293K., pH 5.6, vapor diffusion - sitting drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	chymotrypsin	15 (mg/ml)
2	1	drop	sodium cacodylate	10 (mM)
3	1	drop	cetyltrimethylammonium bromide	0.75 (%sat)
4	1	drop	ammonium sulfate	45 (%sat)
5	1	reservoir	ammonium sulfate	65 (%sat)