Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS.

ABSTRACT: Crystallographic efforts often fail to produce suitably diffracting protein crystals. Unstructured regions of proteins play an important role in this problem and considerable advantage can be gained in removing them. We have developed a number of enhancements to amide hydrogen/high-throughput and high-resolution deuterium exchange MS (DXMS) technology that allow rapid identification of unstructured regions in proteins. To demonstrate the utility of this approach for improving crystallization success, DXMS analysis was attempted on 24 Thermotoga maritima proteins with varying crystallization and diffraction characteristics. Data acquisition and analysis for 21 of these proteins was completed in 2 weeks and resulted in the localization and prediction of several unstructured regions within th

SUBMITTER: Pantazatos D 

PROVIDER: S-EPMC321753 | biostudies-literature | 2004 Jan

REPOSITORIES: biostudies-literature