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Updated: Aug 13, 2026
From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain
H Masumoto1, K Nakagawa, S Irie
1Laboratory of Molecular Structure and Function, Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1--1--1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.
Abstract:
m-Calpain constitutes the prototype of the superfamily of neutral calcium-activated cysteine proteinases. It is a heterodimer consisting of an 80 and a 30 kDa subunit. Recombinant full-length human m-calpain has been crystallized using macro-seeding techniques and vapour-diffusion methods. Two different monoclinic crystal forms (space group P2(1)) were obtained from a solution containing polyethylene glycol (M(W) = 10 000) as a precipitating agent. Complete data sets have been collected to 2.3 and 3.0 A resolution using cryo-cooling conditions and synchrotron radiation. The unit-cell parameters are a = 64.86, b = 133.97, c = 78.00 A, beta = 102.43 degrees and a = 51.80, b = 171.36, c = 64.66 A, beta = 94.78 degrees, respectively. The V(m) values indicate that there is one heterodimer in each asymmetric unit.
