Related Experiment Video
Updated: Jun 24, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
Published on: January 10, 2018
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of YvoA from Bacillus
Marcus Resch1, Heide Marie Roth, Mathias Kottmair
1Lehrstuhl für Biotechnik, Department of Biology, Friederich-Alexander University Erlangen-Nuremberg, Erlangen, Germany.
Abstract:
The putative transcriptional regulator protein YvoA (BSU35030) from Bacillus subtilis was cloned and heterologously expressed in Escherichia coli. The protein was purified by immobilized metal-affinity chromatography and size-exclusion chromatography and subsequently crystallized. A complete native data set was collected to 2.50 A resolution. The crystals belonged to the monoclinic space group C2 and preliminary analysis of the diffraction data indicated the presence of approximately 12 molecules per asymmetric unit.

