Unknown

Dataset Information

0

Protein surface shielding agents in protein crystallization.


ABSTRACT: The molecules adhering temporarily on the surface of protein molecules change the propensity of protein molecules to deposit on the crystal surface in a definite position and orientation. The concepts of competitive adhesion modes and protein surface shielding agents acting on the surface of molecules in a non-equilibrium process of protein crystallization provide a useful platform for the control of crystallization. The desirable goal, i.e. a transient preference of a single dominating adhesion mode between protein molecules during crystallization, leads to uniform deposition of proteins in a crystal. This condition is the most important factor for diffraction quality and thus also for the accuracy of protein structure determination. The presented hypothesis is a generalization of the experimentally well proven behaviour of hydrophilic polymers on the surface of protein molecules of other compounds.

SUBMITTER: Hasek J 

PROVIDER: S-EPMC3004254 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Protein surface shielding agents in protein crystallization.

Hašek J J  

Journal of synchrotron radiation 20101105 1


The molecules adhering temporarily on the surface of protein molecules change the propensity of protein molecules to deposit on the crystal surface in a definite position and orientation. The concepts of competitive adhesion modes and protein surface shielding agents acting on the surface of molecules in a non-equilibrium process of protein crystallization provide a useful platform for the control of crystallization. The desirable goal, i.e. a transient preference of a single dominating adhesion  ...[more]

Similar Datasets

| S-EPMC2034409 | biostudies-literature
| PRJEB74081 | ENA
| S-EPMC6588578 | biostudies-literature
| S-EPMC6955313 | biostudies-literature
| S-EPMC2974831 | biostudies-literature
| S-EPMC3144791 | biostudies-literature
| S-EPMC4188098 | biostudies-literature
| S-EPMC4498707 | biostudies-literature
| S-EPMC2868234 | biostudies-literature
| S-EPMC5783950 | biostudies-literature