CHYMOTRYPSINOGEN: INCREASED RESOLUTION AND ABSOLUTE CONFIGURATION
- 1 May 1964
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 51 (5) , 839-845
- https://doi.org/10.1073/pnas.51.5.839
Abstract
A new set of Fourier maps have been calculated for type F chymotrypsinogen from phases obtained by mul-tiple isomorphous replacement, including terms out to a minimum Bragg spacing of 4 A. Features can now be seen which seem to be in-dividual curved backbone chains with side-chain bulges. There is nothing which would correspond to an [alpha]-helix segment of more than a single turn. Disulfide bridges are still not obvious, and it is still not possible to follow a unique path for the backbone chain. The absolute configuration of the chymotrypsinogen molecule has been established with the aid of anomalous scattering data from the Hg14[long dash]derivative. The correct configuration is the mirror image of our previously pub-lished model. It appears unlikely that our present heavy-atom derivatives would enable the resolution to be extended much further. Possible approaches to the complete structure are discussed.Keywords
This publication has 4 references indexed in Scilit:
- X-ray Analysis of HemoglobinScience, 1963
- Myoglobin and the Structure of ProteinsScience, 1963
- Side-chain interactions in myoglobin.1962
- CHYMOTRYPSINOGEN: A THREE-DIMENSIONAL FOURIER SYNTHESIS AT 5 å RESOLUTIONProceedings of the National Academy of Sciences, 1962