Crystallization and preliminary X-ray analysis of wild-type and V103L mutant Myb R2 DNA-binding domain

Tahir H Tahirov, Hisayuki Morii, Hatsuho Uedaira, Akinori Sarai, Kazuhiro Ogata

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The R2 subdomain of the mouse c-Myb DNA-binding domain and its V103L mutant have been crystallized by the vapour-diffusion method using highly concentrated sodium citrate at pH 6.8 as a precipitant. Using ammonium sulfate as precipitant in MES buffer only produced crystals for the mutant R2. All crystals are isomorphous and belong to space group P212121. The unit-cell dimensions for wild-type R2 crystals grown from sodium citrate precipitant are a = 28.83, b = 40.18, c = 49.23 Å. Crystals contain one R2 molecule per asymmetric unit. They are stable during 3 d exposure to X-rays and diffract to 1.371.45 Å resolution.

Original languageEnglish (US)
Pages (from-to)1345-1347
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number7
DOIs
StatePublished - Jul 1 1999

Fingerprint

X ray analysis
Crystallization
deoxyribonucleic acid
X-Rays
crystallization
Crystals
DNA
Ammonium Sulfate
citrates
crystals
Buffers
x rays
sodium
ammonium sulfates
mice
buffers
Vapors
vapors
X rays
Molecules

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

Crystallization and preliminary X-ray analysis of wild-type and V103L mutant Myb R2 DNA-binding domain. / Tahirov, Tahir H; Morii, Hisayuki; Uedaira, Hatsuho; Sarai, Akinori; Ogata, Kazuhiro.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 55, No. 7, 01.07.1999, p. 1345-1347.

Research output: Contribution to journalArticle

Tahirov, Tahir H ; Morii, Hisayuki ; Uedaira, Hatsuho ; Sarai, Akinori ; Ogata, Kazuhiro. / Crystallization and preliminary X-ray analysis of wild-type and V103L mutant Myb R2 DNA-binding domain. In: Acta Crystallographica Section D: Biological Crystallography. 1999 ; Vol. 55, No. 7. pp. 1345-1347.
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