Alexander V. Zhdanov

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The crystallographic refinement of pepsin structure at 2 A resolution is described. Real space refinement and Jack and Levitt methods were used. As a result, the refined atomic coordinates of 2436 nonhydrogen atoms were obtained. Values of crystallographic R-factor and conformational energy are 29.2% and -1347 kcal/mol correspondingly. The most important(More)
In parallel with crystallographic studies of ribosomes from Thermus thermophilus, a long-term program on the crystallization and structural investigations of ribosomal proteins from the same microorganism has been started at the Institute of Protein Research (Pushchino, Russia). At present, more than half of the individual ribosomal proteins from T(More)
Mitochondrial uncoupling is implicated in many patho(physiological) states. Using confocal live cell imaging and an optical O2 sensing technique, we show that moderate uncoupling of the mitochondria with plecomacrolide Baf (bafilomycin A1) causes partial depolarization of the mitochondria and deep sustained deoxygenation of human colon cancer HCT116 cells(More)
The results of histological examinations of gastric biopsies are presented; over 20% of the biopsies are sent for examinations with the diagnosis of cancer of suspected cancer of the stomach. Histological examinations of gastrobiopsies confirm only 62% of definite endoscopic diagnoses of gastric cancer which is explained either by a wrong choice of the(More)
The determination of the three dimensional structure of chymosin at 3 A resolution by molecular replacement method is described. The rotation functions for various aspartic proteases were calculated and combined results were used for the refinement of orientational parameters of chymosin molecules in the unit cell. The interpretation of Crowther-Blow(More)
The paper is a brief account of aspartic proteinases' structural studies developed in V.A. Engelhardt Institute of Molecular Biology during the last 3 years. The work on porcine pepsin has been finalized after the refinement of the monoclinic crystal form at 1.8 A resolution performed in collaboration with the group of protein structure and function studies(More)
The structure of 3'-methylamino-2',3'-dideoxyribosylthymine [ddT(3'NHMe)] was determined by X-ray analysis. The space group is P2(1)2(1)2(1). Cell dimensions are: a 5.132(1), b 13.718(1), c 16.947(2) A, V 1193.2 A3, Z 4. The structure was solved by directed methods and refined by the full-matrix least square method to R 4.8%. The molecule of ddT(3'NHMe) has(More)