High-resolution crystals of the HU mutant K38N from Bacillus stearothermophilus.
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 A, b = 43.5 A, c = 63.7 A, and beta = 135.1 degrees, and it diffracts x rays to 1.5-A resolution. The second form belongs to the tetragonal space group I41 with a = b = 62.6 A and c = 43.3 A, and it diffracts up to 1.8-A resolution.
Tominaga
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T
Graduate School of Science, Hokkaido University, Sapporo, 060-0810, Japan.
Nakagawa
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A
Tanaka
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I
Kawamura
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S
Kimura
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M
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D001411:Geobacillus stearothermophilus / Q000737:chemistry*; D010316:Particle Size; D013696:Temperature
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C040330:histone-like protein HU, bacteria