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Crystallization and preliminary X‐ray crystallographic studies of nonhistone region of macroH2A.1
Author(s) -
Senadhi VijayKumar,
Chandra Naveen,
Dharia Chhaya,
Pehrson John R.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340220311
Subject(s) - crystallization , crystallography , materials science , x ray crystallography , chemistry , physics , diffraction , optics , thermodynamics
Histone macroH2A has a novel hybrid structure consisting of a large nonhistone region and a region that closely resembles a full‐length histone H2A. One key to understanding macroH2A function is determining the structure and function of its nonhistone region. The nonhistone region of one of the two known macroH2A subtypes was expressed in Escherichia coli and purified using affinity and molecular sieve chromatography. Crystals of the protein suitable for structural studies were grown from polyethylene glycol solutions by vapor equilibration techniques. The crystals belong to the hexagonal space group P6 4 (or its enantiomorph P6 2 ) with unit cell parameters: a = b = 106.2 Å, c = 125.9 Å, α = β = 90°, and γ = 120°. There are four molecules in the asymmetric unit. Self‐rotation function studies revealed three twofold noncrystallographic rotation axes related approximately by 222 symmetry. These crystals have 47% solvent content and diffract to 3.8 Å resolution. © 1995 Wiley‐Liss, Inc.