TY - JOUR
T1 - A new crystal form of photolyase (photoreactivating enzyme) from the cyanobacterium anacystis nidulans
AU - Tamada, Taro
AU - Nishida, Hirokazu
AU - Inaka, Koji
AU - Yasui, Akira
AU - de Ruiter, Petra E.
AU - Eker, Andre P.M.
AU - Miki, Kunio
PY - 1995/7
Y1 - 1995/7
N2 - A new trigonal crystal form of photolyase from the cyanobacterium Anacystis nidulans has been obtained by the addition of ethylenediaminetetra-acetate to the crystallization condition previously used for the tetragonal crystals. In contrast with the tetragonal form that is grown as assemblies of small single crystals, isolated large single crystals were obtained for the present trigonal form, thus providing a regular supply of crystals for X-ray diffraction work. The new form of crystal belongs to the space group P3121 or P3221 with unit cell dimensions of a = b = 146 Å and c = 134 Å. Assuming that the asymmetric unit contains two or three molecules, the Vm value is calculated as 3.9 or 2.6 Å3/Da, respectively. The present crystals diffract X-ray beyond 3.0 Å resolution with synchrotron radiation and were stable toward X-ray exposure.
AB - A new trigonal crystal form of photolyase from the cyanobacterium Anacystis nidulans has been obtained by the addition of ethylenediaminetetra-acetate to the crystallization condition previously used for the tetragonal crystals. In contrast with the tetragonal form that is grown as assemblies of small single crystals, isolated large single crystals were obtained for the present trigonal form, thus providing a regular supply of crystals for X-ray diffraction work. The new form of crystal belongs to the space group P3121 or P3221 with unit cell dimensions of a = b = 146 Å and c = 134 Å. Assuming that the asymmetric unit contains two or three molecules, the Vm value is calculated as 3.9 or 2.6 Å3/Da, respectively. The present crystals diffract X-ray beyond 3.0 Å resolution with synchrotron radiation and were stable toward X-ray exposure.
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U2 - 10.1006/jsbi.1995.1027
DO - 10.1006/jsbi.1995.1027
M3 - Article
AN - SCOPUS:0028874621
VL - 115
SP - 37
EP - 40
JO - Journal of Structural Biology
JF - Journal of Structural Biology
SN - 1047-8477
IS - 1
ER -