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  • 1
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    Mesozooplankton during Professor Vodyanitskiy cruise PV45 (2008)
    PANGAEA
    In:  Institute of Biology of the Southern Seas, National Academy of Sciences of Ukraine, Sevastopol
    Details
    Publication Date: 2023-03-07
    Keywords: Black Sea; CT; DATE/TIME; Depth, bottom/max; Depth, top/min; DEPTH, water; LATITUDE; LONGITUDE; Noctiluca miliaris; Noctiluca miliaris, biomass; Pleurobrachia pileus; Pleurobrachia pileus, biomass; Professor Vodyanitskiy; PV45; PV45-track; Sample code/label; SESAME; Southern European Seas: Assessing and Modelling Ecosystem Changes; Underway cruise track measurements; Zooplankton; Zooplankton, biomass
    Type: Dataset
    Format: text/tab-separated-values, 27 data points
    Location Call Number Expected Availability
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    DATA PANGAEA
  • 2
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    The Global Plankton Database: an inventory and data from the Former Soviet Union expeditions
    PANGAEA
    Details
    Publication Date: 2023-05-12
    Description: At present time, there is a lack of knowledge on the interannual climate-related variability of zooplankton communities of the tropical Atlantic, central Mediterranean Sea, Caspian Sea, and Aral Sea, due to the absence of appropriate databases. In the mid latitudes, the North Atlantic Oscillation (NAO) is the dominant mode of atmospheric fluctuations over eastern North America, the northern Atlantic Ocean and Europe. Therefore, one of the issues that need to be addressed through data synthesis is the evaluation of interannual patterns in species abundance and species diversity over these regions in regard to the NAO. The database has been used to investigate the ecological role of the NAO in interannual variations of mesozooplankton abundance and biomass along the zonal array of the NAO influence. Basic approach to the proposed research involved: (1) development of co-operation between experts and data holders in Ukraine, Russia, Kazakhstan, Azerbaijan, UK, and USA to rescue and compile the oceanographic data sets and release them on CD-ROM, (2) organization and compilation of a database based on FSU cruises to the above regions, (3) analysis of the basin-scale interannual variability of the zooplankton species abundance, biomass, and species diversity.
    Keywords: AAK106; AAK62; AAK65; AAK7/1; AAK7/2; AAK7/3; AAK7/4; AAK7/5; AAK71; AAK88; AAK90; AAK95; Adriatic Sea; Aegean Sea; Akademik A Kovalyevskiy; Akademik Vernadsky; AKov_106-track; AKov_62-track; AKov_65-track; AKov_7/1-track; AKov_7/2-track; AKov_7/3-track; AKov_7/4-track; AKov_7/5-track; AKov_71-track; AKov_88-track; AKov_90-track; AKov_95-track; Arabian Sea; Aral_Sea; Atlantic Ocean; AV10; AV10_938-1; AV10_938-2; AV10_939-1; AV10_939-2; AV10_940-1; AV10_940-2; AV10_941-1; AV10_941-2; AV10_942-1; AV10_942-2; AV10_943-1; AV10_943-2; AV10_944-1; AV10_944-2; AV10_945-1; AV10_945-2; AV10_946-1; AV10_947-1; AV10_948-1; AV10_948-2; AV10_949-1; AV10_949-2; AV10_950-1; AV10_950-2; AV10_950-3; AV10_950-4; AV10_951-1; AV10_951-2; AV10_952-1; AV10_952-2; AV10_953-1; AV10_953-2; AV10_954-1; AV10_954-2; AV10_955-1; AV10_955-2; AV10_956-1; AV10_956-2; AV10_957-1; AV10_958-1; AV10_959-1; AV10_960-1; AV10_961-1; AV10_961-10; AV10_961-100; AV10_961-101; AV10_961-102; AV10_961-103; AV10_961-104; AV10_961-105; AV10_961-106; AV10_961-107; AV10_961-108; AV10_961-109; AV10_961-11; AV10_961-110; AV10_961-111; AV10_961-112; AV10_961-113; AV10_961-114; AV10_961-115; AV10_961-116; AV10_961-117; AV10_961-118; AV10_961-119; AV10_961-12; AV10_961-120; AV10_961-121; AV10_961-122; AV10_961-123; AV10_961-124; AV10_961-125; AV10_961-126; AV10_961-127; AV10_961-128; AV10_961-129; AV10_961-13; AV10_961-130; AV10_961-131; AV10_961-132; AV10_961-133; AV10_961-134; AV10_961-135; AV10_961-136; AV10_961-137; AV10_961-138; AV10_961-139; AV10_961-14; AV10_961-140; AV10_961-141; AV10_961-142; AV10_961-143; AV10_961-144; AV10_961-145; AV10_961-146; AV10_961-147; AV10_961-148; AV10_961-149; AV10_961-15; AV10_961-150; AV10_961-151; AV10_961-152; AV10_961-153; AV10_961-154; AV10_961-155; AV10_961-156; AV10_961-157; AV10_961-158; AV10_961-159; AV10_961-16; AV10_961-160; AV10_961-161; AV10_961-162; AV10_961-163; AV10_961-164; AV10_961-165; AV10_961-166; AV10_961-167; AV10_961-168; AV10_961-169; AV10_961-17; AV10_961-170; AV10_961-171; AV10_961-172; AV10_961-173; AV10_961-174; AV10_961-175; AV10_961-176; AV10_961-177; AV10_961-178; AV10_961-179; AV10_961-18; AV10_961-180; AV10_961-181; AV10_961-182; AV10_961-183; AV10_961-184; AV10_961-185; AV10_961-186; AV10_961-187; AV10_961-188; AV10_961-189; AV10_961-19; AV10_961-190; AV10_961-191; AV10_961-192; AV10_961-193; AV10_961-194; AV10_961-195; AV10_961-196; AV10_961-197; AV10_961-198; AV10_961-199; AV10_961-2; AV10_961-20; AV10_961-200; AV10_961-201; AV10_961-202; AV10_961-203; AV10_961-204; AV10_961-205; AV10_961-206; AV10_961-207; AV10_961-208; AV10_961-209; AV10_961-21; AV10_961-210; AV10_961-211; AV10_961-212; AV10_961-213; AV10_961-214; AV10_961-215; AV10_961-216; AV10_961-217; AV10_961-218; AV10_961-219; AV10_961-22; AV10_961-220; AV10_961-221; AV10_961-222; AV10_961-223; AV10_961-224; AV10_961-225; AV10_961-226; AV10_961-227; AV10_961-228; AV10_961-229; AV10_961-23; AV10_961-230; AV10_961-231; AV10_961-232; AV10_961-233; AV10_961-234; AV10_961-235; AV10_961-236; AV10_961-237; AV10_961-238; AV10_961-239; AV10_961-24; AV10_961-240; AV10_961-241; AV10_961-242; AV10_961-243; AV10_961-244; AV10_961-245; AV10_961-246; AV10_961-247; AV10_961-248; AV10_961-249; AV10_961-25; AV10_961-250; AV10_961-251; AV10_961-252; AV10_961-253; AV10_961-254; AV10_961-255; AV10_961-256; AV10_961-257; AV10_961-258; AV10_961-259; AV10_961-26; AV10_961-260; AV10_961-261; AV10_961-262; AV10_961-263; AV10_961-264; AV10_961-265; AV10_961-266; AV10_961-267; AV10_961-268; AV10_961-269; AV10_961-27; AV10_961-270; AV10_961-271; AV10_961-272; AV10_961-273; AV10_961-274; AV10_961-275; AV10_961-276; AV10_961-277; AV10_961-2771; AV10_961-278; AV10_961-279; AV10_961-28; AV10_961-280; AV10_961-281; AV10_961-282; AV10_961-283; AV10_961-284; AV10_961-285; AV10_961-286; AV10_961-287; AV10_961-288; AV10_961-289; AV10_961-29; AV10_961-290; AV10_961-291; AV10_961-292; AV10_961-293; AV10_961-294; AV10_961-295; AV10_961-296; AV10_961-297; AV10_961-298; AV10_961-299; AV10_961-3; AV10_961-30; AV10_961-300; AV10_961-301; AV10_961-302; AV10_961-303; AV10_961-304; AV10_961-305; AV10_961-306; AV10_961-307; AV10_961-308; AV10_961-309; AV10_961-31; AV10_961-310; AV10_961-311; AV10_961-312; AV10_961-313; AV10_961-314; AV10_961-315; AV10_961-316; AV10_961-317; AV10_961-318; AV10_961-319; AV10_961-32; AV10_961-320; AV10_961-321; AV10_961-322; AV10_961-323; AV10_961-324; AV10_961-325; AV10_961-326; AV10_961-327; AV10_961-328; AV10_961-329; AV10_961-33; AV10_961-330; AV10_961-331; AV10_961-332; AV10_961-333; AV10_961-334; AV10_961-34; AV10_961-35; AV10_961-36; AV10_961-37; AV10_961-38; AV10_961-39; AV10_961-4; AV10_961-40; AV10_961-41; AV10_961-42; AV10_961-43; AV10_961-44; AV10_961-45; AV10_961-46; AV10_961-47; AV10_961-48; AV10_961-49; AV10_961-5; AV10_961-50; AV10_961-51; AV10_961-52; AV10_961-53; AV10_961-54; AV10_961-55; AV10_961-56; AV10_961-57; AV10_961-58; AV10_961-59; AV10_961-6; AV10_961-60; AV10_961-61; AV10_961-62; AV10_961-63; AV10_961-64; AV10_961-65; AV10_961-66; AV10_961-67; AV10_961-68; AV10_961-69; AV10_961-7; AV10_961-70; AV10_961-71; AV10_961-72; AV10_961-73; AV10_961-74; AV10_961-75; AV10_961-76; AV10_961-77; AV10_961-78; AV10_961-79; AV10_961-8; AV10_961-80; AV10_961-81; AV10_961-82; AV10_961-83; AV10_961-84; AV10_961-85; AV10_961-86; AV10_961-862; AV10_961-87; AV10_961-88; AV10_961-89; AV10_961-9; AV10_961-90; AV10_961-91; AV10_961-92; AV10_961-93; AV10_961-94; AV10_961-95; AV10_961-96; AV10_961-97; AV10_961-98; AV10_961-99; AV10_962-1; AV10_963-1; AV10_964-1; AV10_965-1; AV10_966-1; AV10_967-1; AV10_968-2; AV10_969-2; AV10_970-1; AV10_970-2; AV10_971-2; AV10_974-1; AV11; AV11_1000-2; AV11_1001-2; AV11_1002-2; AV11_1003-1; AV11_1005-1; AV11_1006-1; AV11_1006-10; AV11_1006-11; AV11_1006-12; AV11_1006-13; AV11_1006-15; AV11_1006-16; AV11_1006-17; AV11_1006-18; AV11_1006-19; AV11_1006-2; AV11_1006-20; AV11_1006-21; AV11_1006-22; AV11_1006-23; AV11_1006-24; AV11_1006-25; AV11_1006-26; AV11_1006-27; AV11_1006-28; AV11_1006-29; AV11_1006-3; AV11_1006-30; AV11_1006-31; AV11_1006-32; AV11_1006-33; AV11_1006-34; AV11_1006-35; AV11_1006-36; AV11_1006-37; AV11_1006-38; AV11_1006-39; AV11_1006-4; AV11_1006-40; AV11_1006-41; AV11_1006-42; AV11_1006-43; AV11_1006-44; AV11_1006-45; AV11_1006-46; AV11_1006-47; AV11_1006-48; AV11_1006-49; AV11_1006-5; AV11_1006-50; AV11_1006-51; AV11_1006-52; AV11_1006-6; AV11_1006-7; AV11_1006-8; AV11_1006-9; AV11_1007-10; AV11_1007-11; AV11_1007-12; AV11_1007-13; AV11_1007-14; AV11_1007-15; AV11_1007-16; AV11_1007-17; AV11_1007-18; AV11_1007-19; AV11_1007-2; AV11_1007-20; AV11_1007-21; AV11_1007-22; AV11_1007-23; AV11_1007-24; AV11_1007-25; AV11_1007-26; AV11_1007-27; AV11_1007-28; AV11_1007-29; AV11_1007-3; AV11_1007-30; AV11_1007-31; AV11_1007-32; AV11_1007-33; AV11_1007-34; AV11_1007-35; AV11_1007-36; AV11_1007-37; AV11_1007-38; AV11_1007-39; AV11_1007-4; AV11_1007-40; AV11_1007-41; AV11_1007-42; AV11_1007-43; AV11_1007-44; AV11_1007-45; AV11_1007-46; AV11_1007-47; AV11_1007-48; AV11_1007-49; AV11_1007-5; AV11_1007-50; AV11_1007-51; AV11_1007-52; AV11_1007-53; AV11_1007-54; AV11_1007-55; AV11_1007-56; AV11_1007-57; AV11_1007-58; AV11_1007-59; AV11_1007-6; AV11_1007-60; AV11_1007-61; AV11_1007-62; AV11_1007-63; AV11_1007-7; AV11_1007-8; AV11_1007-9; AV11_1008-1; AV11_1010-1; AV11_1010-2; AV11_1011-1; AV11_1011-2; AV11_1012-1; AV11_1013-1; AV11_1013-2; AV11_1014-1; AV11_1014-2; AV11_1015-1; AV11_1015-2; AV11_1016-1; AV11_1016-2; AV11_1017-1; AV11_1017-2; AV11_1018-1; AV11_1018-2; AV11_1019-1; AV11_1019-2; AV11_1021-2; AV11_1022-2; AV11_1023-2; AV11_1024-2; AV11_1025-2; AV11_1026-2; AV11_1027-2; AV11_1028-2; AV11_1029-2; AV11_1030-2; AV11_1032-2; AV11_1033-2; AV11_1034-2; AV11_1035-2; AV11_1036-2; AV11_1037-2; AV11_1038-2; AV11_1039-2; AV11_1040-2; AV11_1041-2; AV11_1042-2; AV11_1043-2; AV11_1044-2; AV11_1045-2; AV11_1046-2; AV11_1051-1; AV11_1051-10; AV11_1051-11; AV11_1051-12; AV11_1051-13; AV11_1051-14; AV11_1051-15; AV11_1051-16; AV11_1051-17; AV11_1051-18;
    Type: Dataset
    Format: application/zip, 752 datasets
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    DATA PANGAEA
  • 3
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray study of β-mannosidase from Trichoderma reesei (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 342-343 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: β-Mannosidase from Trichoderma reesei, a 105 kDa glycoprotein, has been crystallized. The crystals belong to the space group P41212 or P43212, with unit-cell dimensions a = b = 165.86, c = 122.46 Å, and diffract beyond 2.75 Å resolution. X-ray diffraction data were collected from a frozen crystal on a synchrotron X-ray source.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999016625
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    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray study of haem-binding protein from the bloodsucking insect Rhodnius prolixus (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 860-861 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Rhodnius haem-binding protein (RHBP) from the bloodsucking insect Rhodnius prolixus, a 15 kDa protein, has been crystallized using polyethylene glycol as a precipitant. X-ray diffraction data have been collected at a synchrotron source. The crystals belong to the space group P41(3)212, with unit-cell parameters a = b = 64.98, c = 210.68 Å, and diffract beyond 2.6 Å resolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901004437
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray diffraction studies of piratoxin II, a phospholipase A2 isolated from the venom of Bothrops pirajai (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 1437-1439 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The phospholipases A2 (PLA2, E.C. 3.1.1.4, phosphatide sn2 acylhydrolases) are the major components of the venom of several snakes. They are responsible for several important pharmacological effects observed in ophidian incidents. PLA2 piratoxin II from Bothrops pirajai has been crystallized by the vapour-diffusion technique. X-ray diffraction data have been collected to 2.04 Å resolution (90.2% complete, Rmerge = 0.070). The space group is P21 and the cell parameters are a = 46.19, b = 60.36, c = 58.74 Å and β = 96.05°. The structure has been solved by molecular replacement using the crystallographic structure of PLA2 from Bothrops asper (PDB code 1CLP) as a search model.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998007082
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary diffraction studies of a recombinant major urinary protein (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1340-1341 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A monoclinic crystal form of a recombinant major urinary protein, (MUP) from mouse, has been obtained. MUP is a member of the lipocalin family whose biological function relates to olfaction and sexual communication. Crystals were grown by the vapour-diffusion technique against a mother liquor containing CdCl2. Crystals belong to the monoclinic space group P21 with the cell parameters a = 37.14, b = 55.79, c = 37.67 Å, and β = 93.24°. The crystals diffract to beyond 1.4 Å resolution at a synchrotron beamline.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999005661
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Purification, crystallization and preliminary crystallographic study of a Kunitz-type trypsin inhibitor from Delonix regia seeds (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1611-1613 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The Kunitz-type trypsin inhibitor from seeds of Flamboyant (Delonix regia) has been purified to homogeneity and plate-like crystals suitable for X-ray analysis have been grown by the hanging-drop method using PEG 6000 as a precipitant. The crystals belong to space group P212121 with unit-cell parameters a = 32.15, b = 69.39, c = 72.54 Å. X-ray diffraction data have been collected to 2.95 Å resolution. The structure has been solved by molecular replacement using the known structures of trypsin inhibitors from Erythrina caffra seeds (PDB code 1tie) and from soya beans (Glycine max; PDB code 1ba7) as search models.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999009361
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  • 8
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray diffraction studies of human catalase (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1614-1615 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The enzyme catalase (H2O2–H2O2 oxidoreductase; E.C. 11.1.6) was purified from haemolysate of human placenta and crystallized using the vapour-diffusion technique. Synchrotron-radiation diffraction data have been collected to 1.76 Å resolution. The enzyme crystallized in the space group P212121, with unit-cell dimensions a = 83.6, b = 139.4, c = 227.5 Å. A molecular-replacement solution of the structure has been obtained using beef liver catalase (PDB code 4blc) as a search model.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999009695
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  • 9
    Electronic Resource
    Electronic Resource
    Preparation and preliminary X-ray diffraction studies of a new crystal form of L-asparaginase from Escherichia coli (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1616-1617 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: L-Asparaginase is an enzyme which hydrolyzes asparagine to produce aspartic acid and ammonia. It is an effective chemotherapeutic drug, especially in the treatment of acute lymphoblastic leukaemia in children. The enzyme from Escherichia coli was crystallized in a new crystal form with space group C2, unit-cell parameters a = 76.3 (0), b = 134.6 (2), c = 64.8 (7) Å, β = 110.5 (1)° and a dimer in the asymmetric unit. Synchrotron-radiation diffraction data have been collected to 1.95 Å resolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S090744499901001X
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  • 10
    Electronic Resource
    Electronic Resource
    Purification, crystallization and preliminary diffraction study of β-galactosidase from Penicillium sp. (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 1508-1509 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Crystals of an extracellular β-galactosidase from Penicillium sp. (MW = 120 ± 5 kDa) have been obtained from a sodium phosphate buffer using PEG as precipitant. The crystals belong to the tetragonal space group P41or P43, with unit-cell parameters a = b = 110.82, c = 161.28 Å, and diffract to 1.85 Å resolution at a synchrotron source.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900011756
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