TY - JOUR
T1 - A low-resolution study of testicular lactate dehydrogenase using the molecular replacement technique
AU - Donald, W.
AU - Musick, L.
AU - Adams, April D.
AU - Rossmann, Michael G.
AU - Wheat, Thomas E.
AU - Goldberg, Erwin
N1 - Funding Information:
The authors acknowledge the expert advice and assist$ancch of Drs G. C. E’ord ancl L. L. Reed, and t)he outstanding technical assistanr(x given by Sharon Wilder in thf, preparat,ion of the manuscript. The work at Purdue was supported by a National lnsti-tutes of Health grant (no. GM 10704) and a National Science Foundation grant (no. BMS74-23537), while the work at Northwestern Universit)y was supported by a National Institutes of Health grant (no. HD 05863).
PY - 1976/7/5
Y1 - 1976/7/5
N2 - 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.
AB - 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.
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U2 - 10.1016/0022-2836(76)90127-3
DO - 10.1016/0022-2836(76)90127-3
M3 - Article
C2 - 950672
AN - SCOPUS:0017064551
SN - 0022-2836
VL - 104
SP - 659
EP - 668
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 3
ER -