Effect assessment for the interaction between shaking table and eccentric load.

Electro-hydraulic shaking table is an essential experimental apparatus to evaluate structural performance under actual vibration condition. The control-structure interaction (CSI) between shaking table and eccentric load has lately received considerable attention for causing the accuracy degradation of shaking table test. At present, the research gap of the influence of the eccentricity of load on the CSI makes it challenging to find the CSI effects. And an effect assessment is yet to be proposed to evaluate the CSI effects, which has impeded the development of test technology. To overcome those theoretical bottlenecks, in this research, an analytical transfer function matrix of shaking table and eccentric load is established to analyze the CSI effects. The analysis is conducted under such conditions as different mass ratio (MR), moment of inertia ratio (IR), and eccentric distance ratio (ER) conditions. Through the analysis, the role of the ER is identified, the sensitivities of the MR, IR, and ER to the transfer function matrix are revealed, and the CSI effects are found. Furthermore, a novelty effect assessment is proposed to appraise whether the CSI effects can be ignored in shaking table test. And the visualization expression of the effect assessment is obtained for convenient application.

The N-terminus of FILIA forms an atypical KH domain with a unique extension involved in interaction with RNA.

FILIA is a member of the recently identified oocyte/embryo expressed gene family in eutherian mammals, which is characterized by containing an N-terminal atypical KH domain. Here we report the structure of the N-terminal fragment of FILIA (FILIA-N), which represents the first reported three-dimensional structure of a KH domain in the oocyte/embryo expressed gene family of proteins. The structure of FILIA-N revealed a unique N-terminal extension beyond the canonical KH region, which plays important roles in interaction with RNA. By co-incubation with the lysates of mice ovaries, FILIA and FILIA-N could sequester specific RNA components, supporting the critical roles of FILIA in regulation of RNA transcripts during mouse oogenesis and early embryogenesis.

Preliminary crystallographic analysis of the N-terminal domain of FILIA, a protein essential for embryogenesis.

FILIA is a component of the subcortical maternal complex that is essential for early stage embryogenesis. Its 6xHis-tagged N-terminal domain was expressed in Escherichia coli and purified to homogeneity. Two types of crystals formed under different crystallization conditions during screening. Orthorhombic crystals appeared in a solution containing 1.4 M ammonium sulfate, 0.1 M Tris pH 8.2 and 12% glycerol, while tetragonal crystals were obtained using 15% PEG 4000 mixed with 0.1 M HEPES pH 7.5 and 15% 2-propanol. High-quality diffraction data were collected from the two crystal forms to resolutions of 1.8 and 2.2 A, respectively, using synchrotron radiation. The Matthews coefficients indicated that the P2(1)2(1)2(1) and P4(1)2(1)2 crystals contained two molecules and one molecule per asymmetric unit, respectively. A selenomethionine-substituted sample failed to crystallize under the native conditions, but another orthorhombic crystal form was obtained under different conditions and anomalous diffraction data were collected.