Structure of bovine trypsinogen at 1.9 Å resolution
- 22 February 1977
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 16 (4), 654-664
- https://doi.org/10.1021/bi00623a016
Abstract
The 3-dimensional crystal structure of bovine trypsinogen at .apprx. pH 7.5 was initially solved at 2.6 .ANG. resolution using the multiple isomorphous replacement method. Preliminary refinement cycles of the atomic coordinates for trypsinogen were carried out first to a resolution of 2.1 .ANG., and later to 1.9 .ANG., using constrained difference Fourier refinement. During the process, structure factors Fc and .phi.c were calculated from the trypsinogen structure and final interpretation was based on an electron-density map computed with terms (2This publication has 5 references indexed in Scilit:
- A detailed structural comparison between the charge relay system in chymotrypsinogen and in α-chymotrypsinBiochemistry, 1976
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1968
- CHROMATOGRAPHY OF TRYPSIN AND ITS DERIVATIVES - CHARACTERIZATION OF A NEW ACTIVE FORM OF BOVINE TRYPSIN1968
- STUDIES ON ACTIVE CENTER OF TRYPSIN - BINDING OF AMIDINES AND GUANIDINES AS MODELS OF SUBSTRATE SIDE CHAIN1965
- IDENTIFICATION OF A PEPTIDE RELEASED DURING AUTOCATALYTIC ACTIVATION OF TRYPSINOGENJournal of Biological Chemistry, 1955