1TMN

Binding of n-carboxymethyl dipeptide inhibitors to thermolysin determined by x-ray crystallography. a novel class of transition-state analogues for zinc peptidases

Experimental procedure

Experimental method	SINGLE CRYSTAL
Source type	ROTATING ANODE
Source details	ELLIOTT GX-21
Temperature [K]	285
Detector technology	FILM
Collection date	1983
Detector	KODAK
Spacegroup name	P 61 2 2
Unit cell lengths	94.200, 94.200, 131.400
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	14.900 - 1.900
Rwork	0.171
Structure solution method	MOLECULAR SUBSTATUTION
RMSD bond length	0.021
RMSD bond angle	3.600
Data reduction software	OSCTST
Data scaling software	AGROVATA/ROTAVATE
Phasing software	RICHARDS (BOX MODELING)
Refinement software	EREF

Data quality characteristics

	Overall
Low resolution limit [Å]	14.900
High resolution limit [Å]	1.700
Rmerge	0.069
Number of reflections	23734

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	7.2		pH 7.2

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	calcium acetate	0.01 (M)
2	1	1	Tris acetate	0.01 (M)
3	1	1	dimethyl sulfoxide	7 (%(v/v))