Related Experiment Video
Updated: Aug 8, 2026
Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Crystallization and preliminary X-ray analysis of cytochrome c-552 from Nitrosomonas europaea
C Nagata1, H Moriyama, T Fujiwara
1Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama.
Abstract:
Cytochrome c-552 from Nitrosomonas europaea was crystallized by the sandwiched drop, vapor diffusion method, with anmmonium sulfate as the precipitant. The crystals were found to belong to the space group P2(1)2(1)2(1), having unit cell dimensions of a = 106.1 A, b = 126.1 A, and c = 57.7 A. The crystals diffracted X-rays at greater than 3.0 A resolution.
More Related Videos
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
10:45Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
Published on: March 20, 2021