A low-resolution study of testicular lactate dehydrogenase using the molecular replacement technique

W. Donald, L. Musick, April D. Adams, Michael G. Rossmann*, Thomas E. Wheat, Erwin Goldberg

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

The orientation of the molecular 2-fold axes of mouse testicular lactate dehydrogenase (LDHase ‡ Abbreviation used: LDHase, lactate dehydrogenase.-C4) was determined by a rotation function search. These were subsequently identified with the P, Q, and R axes of dogfish LDHase-M4. Since LDHase-C4 crystallized with one molecule in a triclinic cell, the origin of the co-ordinate system was arbitrarily fixed at the molecular center. Structure factor phases were derived from an appropriately oriented dogfish apo LDHase-M4 phasing model and combined with the observed structure amplitudes to produce a hybrid electron density map. Density points related by the molecular 222 point symmetry were averaged so as to remove the bias of the phasing model. At 7.5 Å resolution, the structure of the crystallized mouse LDHase-C4 was found to be without coenzyme, with a conformation indistinguishable from that of dogfish apo LDHase-M4.

Original languageEnglish (US)
Pages (from-to)659-668
Number of pages10
JournalJournal of Molecular Biology
Volume104
Issue number3
DOIs
StatePublished - Jul 5 1976

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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