Related Experiment Video
Updated: Jul 31, 2026
Budding Yeast Protein Extraction and Purification for the Study of Function, Interactions, and Post-translational Modifications
Published on: October 30, 2013
Expression, crystallization and preliminary X-ray analysis of the Pyrococcus abyssi protein homologue of
Patrícia Pereira Coltri1, Beatriz Gomes Guimarães, Carla Columbano Oliveira
1Center for Structural Molecular Biology, Brazilian Synchrotron Light Laboratory, LNLS CP 6192, CEP 13084-971, Campinas SP, Brazil.
Abstract:
Saccharomyces cerevisiae Nip7p is a nucleolar protein required for accurate processing of the 27S precursor of the 25S and 5.8S ribosomal RNAs. Nip7p homologues are found in eukaryotes and archaea. The Pyrococcus abyssi homologue of Nip7p (PaNip7) was cloned, expressed in Escherichia coli and purified for crystallization. X-ray diffraction data were collected from native crystals and an iodide derivative using synchrotron radiation. PaNip7 native crystals diffract to 1.8 A and belong to space group C2, with unit-cell parameters a = 88.49, b = 90.28, c = 63.35 A, beta = 134.29 degrees. The PaNip7 structure was solved using the SIRAS method.
More Related Videos
12:23Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
09:15Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
Published on: January 10, 2018