TY - JOUR
T1 - Crystallization and preliminary X-ray study of two crystal forms of Klebsiella oxytoca diol dehydratase-cyanocobalamin complex
AU - Masuda, Jun
AU - Yamaguchi, Tetsuya
AU - Tobimatsu, Takamasa
AU - Toraya, Tetsuo
AU - Suto, Kyoko
AU - Shibata, Naoki
AU - Morimoto, Yukio
AU - Higuchi, Yoshiki
AU - Yasuoka, Noritake
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1999/4
Y1 - 1999/4
N2 - Two crystal forms of Klebsiella oxytoca diol dehydratase complexed with cyanocobalamin have been obtained and preliminary crystallographic experiments have been performed. The crystals belong to two different space groups, depending on the crystallization conditions. One crystal (form I) belongs to space group P212121 with unit-cell parameters a = 76.2, b = 122.3, c = 209.6 Å, and diffracts to 2.2 Å resolution using an X-ray beam from a synchrotron radiation source. The other crystal (form II) belongs to space group P21 with unit-cell parameters a = 75.4, b = 132.7, c = 298.8 Å, β = 91.9°, and diffracts to 3.0 Å resolution. For the purpose of structure determination, a heavy-atom derivative search was carried out and some mercuric derivatives were found to be promising. Structure analysis by the multiple isomorphous replacement method is now under way.
AB - Two crystal forms of Klebsiella oxytoca diol dehydratase complexed with cyanocobalamin have been obtained and preliminary crystallographic experiments have been performed. The crystals belong to two different space groups, depending on the crystallization conditions. One crystal (form I) belongs to space group P212121 with unit-cell parameters a = 76.2, b = 122.3, c = 209.6 Å, and diffracts to 2.2 Å resolution using an X-ray beam from a synchrotron radiation source. The other crystal (form II) belongs to space group P21 with unit-cell parameters a = 75.4, b = 132.7, c = 298.8 Å, β = 91.9°, and diffracts to 3.0 Å resolution. For the purpose of structure determination, a heavy-atom derivative search was carried out and some mercuric derivatives were found to be promising. Structure analysis by the multiple isomorphous replacement method is now under way.
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U2 - 10.1107/S0907444998018356
DO - 10.1107/S0907444998018356
M3 - Article
C2 - 10089331
AN - SCOPUS:0033119955
SN - 0907-4449
VL - 55
SP - 907
EP - 909
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
IS - 4
ER -