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Updated: Jun 18, 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
Crystallization and initial X-ray diffraction study of the three PASTA domains of the Ser/Thr kinase Stk1 from the
Patricia Paracuellos1, Allison Ballandras, Xavier Robert
1Institut de Biologie et Chimie des Protéines, UMR CNRS Université de Lyon, France.
Abstract:
PASTA subunits (approximately 70 amino acids) are specific to bacterial serine/threonine kinases and to penicillin-binding proteins (PBPs) and are involved in the synthesis of peptidoglycan. The human pathogen Staphylococcus aureus contains a serine/threonine kinase, Stk1, which plays a major role in virulence. A recombinant His-tagged portion of the extracellular domain of Stk1 containing three PASTA subunits has been crystallized using zinc sulfate as a crystallizing agent. The crystals belonged to the tetragonal space group P4(1)22, with unit-cell parameters a = 68.0, b = 68.0, c = 158.1 angstrom. Structure determination by the MAD method is now in progress.
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