Use of molecular replacement in the structure determination of the P21212 and the P21 (Pseudo P21212) crystal forms of oxidized uteroglobin |
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Authors: | Manfred Buehner Alain Lifchitz Renée Bally Jean Paul Mornon |
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Institution: | Forschergruppe Roentgenstrukturanalyse, Biologischer Makromoleküle, Universität Würzburg Chemie Zentralgebäude Am Hubland D-8700 Würzburg, Federal Republic of Germany;Laboratoire de Minéralogie-Cristallographie associé au CNRS, Université P. et M. Curie 4 place Jussieu F-75230 Paris Cedex 05, France |
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Abstract: | The structure of the symmetrical dimer of oxidized rabbit Uteroglobin, as determined from the crystal form in space group C2221, has been used as a model to determine the general parameters of this protein in two other crystal forms; namely, a symmetrical dimer in P21212 and an asymmetrical dimer in P21 with non-crystallographic symmetry approaching P21212. Independently, the structure in P21212 was solved by multiple isomorphous replacement.After exchanging data, the analysis was carried out in two different laboratories with different methods of molecular replacement. The result was the same for both approaches, and it could be shown further that the packing of molecules in both crystal forms analysed is so similar that they can be considered pseudoisomorphous, i.e. distinguished only by the fact that two out of three symmetry operators are crystallographically perfect in one case and molecular and approximate only in the other.The principal fold of the polypeptide chain is the same in all crystal forms considered so far, but there is evidence for differences in the detail, which will be worked out later with progressing refinement. |
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