Crystallization and preliminary X-ray analysis of wild-type and V103L mutant Myb R2 DNA-binding domain.
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 A. Crystals contain one R2 molecule per asymmetric unit. They are stable during 3 d exposure to X-rays and diffract to 1.37-1.45 A resolution.
Tahirov
T H
TH
Kanagawa Academy of Science and Technology (KAST), 3-9 Fukuura, Kanazawa-ku, Yokohama 236-0004, Japan.
Morii
H
H
Uedaira
H
H
Sarai
A
A
Ogata
K
K
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D051379:Mice; D009154:Mutation; D011487:Protein Conformation; D011518:Proto-Oncogene Proteins / Q000737:chemistry* / Q000235:genetics; D020598:Proto-Oncogene Proteins c-myb; D015534:Trans-Activators / Q000737:chemistry* / Q000235:genetics
D004268:DNA-Binding Proteins; D011518:Proto-Oncogene Proteins; D020598:Proto-Oncogene Proteins c-myb; D015534:Trans-Activators