Crystallization of scytalone dehydratase F162A mutant in the unligated state and a preliminary X-ray diffraction study at 37 K
書誌事項
- 公開日
- 2001-12-21
- 権利情報
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- http://journals.iucr.org/services/copyrightpolicy.html
- http://journals.iucr.org/services/copyrightpolicy.html#TDM
- DOI
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- 10.1107/s0907444901017371
- 公開者
- International Union of Crystallography (IUCr)
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説明
Scytalone dehydratase variant F162A, in which Phe162 in the C-terminal region was replaced with alanine, was crystallized with polyethylene glycol 4000. Because the crystal was radiation-sensitive, the diffraction data were collected at cryogenic temperatures. The crystal belonged to monoclinic space group P2(1), with unit-cell parameters a = 72.64, b = 61.30, c = 72.62 A, beta = 120.02 degrees at 37 K. The calculated V(M) value was acceptable when a trimer of the mutant enzyme occupied a crystallographic asymmetric unit. The resolution limit was extended to 1.45 A at BL41XU of SPring-8 at 37 K.
収録刊行物
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- Acta Crystallographica Section D Biological Crystallography
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Acta Crystallographica Section D Biological Crystallography 58 (1), 148-150, 2001-12-21
International Union of Crystallography (IUCr)
