1PPE

THE REFINED 2.0 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND CMTI-I, A TRYPSIN INHIBITOR FROM SQUASH SEEDS (CUCURBITA MAXIMA): TOPOLOGICAL SIMILARITY OF THE SQUASH SEED INHIBITORS WITH THE CARBOXYPEPTIDASE A INHIBITOR FROM POTATOES

Experimental procedure

Spacegroup name	P 21 21 21
Unit cell lengths	59.280, 55.470, 74.590
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 2.000
R-factor	0.151 *
Rwork	0.151
RMSD bond length	0.020
RMSD bond angle	2.700
Phasing software	SQUASH
Refinement software	EREF

Data quality characteristics

	Overall
High resolution limit [Å]	2.000 *
Rmerge	0.073 *
Total number of observations	54864 *
Number of reflections	14191 *
Completeness [%]	81.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *		20 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG6000	20 (%)
2	1	reservoir	phosphate	0.1 (M)