High-resolution crystals of the HU mutant K38N from Bacillus stearothermophilus

Takahiro Tominaga, Atsushi Nakagawa, Isao Tanaka, Shunsuke Kawamura, Makoto Kimura

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


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.

Original languageEnglish
Pages (from-to)86-89
Number of pages4
JournalJournal of structural biology
Issue number1
Publication statusPublished - Mar 1999

All Science Journal Classification (ASJC) codes

  • Structural Biology


Dive into the research topics of 'High-resolution crystals of the HU mutant K38N from Bacillus stearothermophilus'. Together they form a unique fingerprint.

Cite this