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Acta Crystallographica Section D: Biological Crystallography (1)
Acta Crystallographica Section F: Structural Biology and Crystallization Communications (1)
Barford, David (1)
Chang, Leifu (1)
Kulkarni, Kiran (1)
Kulkarni, Kiran A. (1)
Lavanya Latha, V. (1)
Nagender Rao, R. (1)
Siva Kumar, N. (1)
Suguna, K. (1)
Yang, Jing (1)
Zhang, Ziguo (1)
da Fonseca, Paula C. A. (1)
Year of Publication
Building a pseudo-atomic model of the anaphase-promoting complex
da Fonseca, Paula C. A.
Acta Crystallographica Section D: Biological Crystallography
This article describes an example of molecular replacement in which atomic models are used to interpret electron-density maps determined using single-particle electron-microscopy data.
The anaphase-promoting complex (APC/C) is a large E3 ubiquitin ligase that regulates progression through specific stages of the cell cycle by coordinating the ubiquitin-dependent degradation of cell-cycle regulatory proteins. Depending on the species, the active form of the APC/C consists of 14–15 different proteins that assemble into a 20-subunit complex with a mass of approximately 1.3 MDa. A hybrid approach of single-particle electron microscopy and protein crystallography of individual APC/C subunits has been applied to generate pseudo-atomic models of various functional states of the complex. Three approaches for assigning regions of the EM-derived APC/C density map to specific APC/C subunits are described. This information was used to dock atomic models of APC/C subunits, determined either by protein crystallography or homology modelling, to specific regions of the APC/C EM map, allowing the generation of a pseudo-atomic model corresponding to 80% of the entire complex.
anaphase-promoting complex; single-particle electron microscopy; pseudo-atomic model
Crystallization and preliminary X-ray crystallographic analysis of a galactose-specific lectin from Dolichos lablab
Lavanya Latha, V.
Nagender Rao, R.
Siva Kumar, N.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
The galactose-specific lectin from the seeds of a leguminous plant, D. lablab, has been crystallized. Molecular-replacement solution using 3.0 Å X-ray diffraction data showed the lectin to be a tetramer.
The galactose-specific lectin from the seeds of Dolichos lablab has been crystallized using the hanging-drop vapour-diffusion technique. The crystals belong to space group P1, with unit-cell parameters a = 73.99, b = 84.13, c = 93.15 Å, α = 89.92, β = 76.01, γ = 76.99°. X-ray diffraction data to a resolution of 3.0 Å have been collected under cryoconditions (100 K) using a MAR imaging-plate detector system mounted on a rotating-anode X-ray generator. Molecular-replacement calculations carried out using the available structures of legume lectins as search models revealed that the galactose-specific lectin from D. lablab forms a tetramer similar to soybean agglutinin; two such tetramers are present in the asymmetric unit.
Dolichos lablab; galactose-specific lectins; legume lectins
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