issue contents

ISSN: 2053-230X

December 2022 issue

Highlighted illustration

Cover illustration: The purine nucleoside phosphorylase from Geobacillus stearothermophilus is a thermostable protein of potential interest for the biocatalytic synthesis of antiviral nucleoside compounds. The structure of the protein was determined and found to include a His tag in the active site [Given et al. (2022), Acta Cryst. F78, 416–422]. This study shows that while tags are useful in the purification of proteins, we need to ensure that they do not have unwanted effects on protein structure and function.

scientific comment

link to html
Is it possible to relate experimental calorimetry measurements of protein ligand binding to 3D structures?

research communications

link to html
Serine palmitoyltransferase (SPT) is the rate-limiting key enzyme in the sphingolipid biosynthetic pathway. Here, the structure of SPT from S. multivorum complexed with tris(hydroxymethyl)aminomethane is reported at 1.65 Å resolution, which is an improvement on the previously reported structure at 2.3 Å resolution.

link to html
The structure of Geobacillus stearothermophilus purine nucleoside phosphorylase, an enzyme of biocatalytic interest, is reported and was found to include the presence of an N-terminal tag in the active site of each subunit that belongs to the other subunit in each dimer. This serves as a warning that while tags enable simple and economic purification for proteins of industrial interest, care needs to be taken to ensure that they do not have unwanted effects on protein structure and function.
Follow Acta Cryst. F
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds