1AFQ

CRYSTAL STRUCTURE OF BOVINE GAMMA-CHYMOTRYPSIN COMPLEXED WITH A SYNTHETIC INHIBITOR

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	292
Detector technology	IMAGE PLATE
Collection date	1995-11-10
Detector	RIGAKU
Spacegroup name	P 42 21 2
Unit cell lengths	69.840, 69.840, 97.360
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	5.000 - 1.800
R-factor	0.181
Rwork	0.181
R-free	0.18200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ab9
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]	97.400	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.059	0.143 *
Total number of observations	215467 *
Number of reflections	22647
<I/σ(I)>	13.5	4.09
Completeness [%]	98.1	94.6 *
Redundancy	9.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	5.6 *	293	GAMMA-CHYMOTRYPSIN CRYSTALS WERE SOAKED INTO A SOLUTION CONTAINING SATURATED INHIBITOR, 65% SATURATED AMMONIUM SULFATE AND 100 MM HEPES BUFFER (PH7.5) AT 293K FOR A MONTH.

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	10.5 (mM)
3	1	drop	cetyltrimethylammonium bromide	0.75 (%sat)
4	1	drop	ammonium sulfate	45 (%sat)
5	1	reservoir	ammonium sulfate	65 (%sat)