TY - JOUR
T1 - High-resolution crystals of the HU mutant K38N from Bacillus stearothermophilus
AU - Tominaga, Takahiro
AU - Nakagawa, Atsushi
AU - Tanaka, Isao
AU - Kawamura, Shunsuke
AU - Kimura, Makoto
N1 - Funding Information:
We thank Professor N. Sakabe, Dr. N. Watanabe, and Dr. M. Suzuki for their help in data collection at the Photon Factory, High Energy Physics Laboratory, Japan. This work was partly supported by the ‘‘Research for the Future’’ Program (JSPS-RFTF 97L00501) from the Japan Society for the Promotion of Science.
PY - 1999/3
Y1 - 1999/3
N2 - The DNA-binding protein HU is ubiquitous in the prokaryotic cell. It is a major protein component of isolated nucleoids and is believed to control the tertiary structure of prokaryotic DNA. The Bacillus stearothermophilus HU (BstHU) mutants obtained by mutagenesis have been investigated. Crystallization experiments of BstHU-K38N (Lys38 is substituted with Asn) resulted in two forms of crystals suitable for high-resolution x-ray analysis. The first form belongs to the monoclinic space group C2 with unit- cell dimensions of a = 90.1 Å, b = 43.5 Å, c = 63.7 Å, and β = 135.1°and it diffracts x rays to 1.5-Å resolution. The second form belongs to the tetragonal space group I41 with a = b = 62.6 Å and c = 43.3 Å, and it diffracts up to 1.8-Å resolution.
AB - The DNA-binding protein HU is ubiquitous in the prokaryotic cell. It is a major protein component of isolated nucleoids and is believed to control the tertiary structure of prokaryotic DNA. The Bacillus stearothermophilus HU (BstHU) mutants obtained by mutagenesis have been investigated. Crystallization experiments of BstHU-K38N (Lys38 is substituted with Asn) resulted in two forms of crystals suitable for high-resolution x-ray analysis. The first form belongs to the monoclinic space group C2 with unit- cell dimensions of a = 90.1 Å, b = 43.5 Å, c = 63.7 Å, and β = 135.1°and it diffracts x rays to 1.5-Å resolution. The second form belongs to the tetragonal space group I41 with a = b = 62.6 Å and c = 43.3 Å, and it diffracts up to 1.8-Å resolution.
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U2 - 10.1006/jsbi.1998.4076
DO - 10.1006/jsbi.1998.4076
M3 - Article
C2 - 10196119
AN - SCOPUS:0032808734
SN - 1047-8477
VL - 125
SP - 86
EP - 89
JO - Journal of structural biology
JF - Journal of structural biology
IS - 1
ER -