9h4a

Ribonuclease-three Like 4 crystallization and structure determination at room temperature in the CrystalChip

spinqualitylabelsall models 9h4a, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9h4a is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NFD2_ARATH Required for karyogamy during female gametophyte development, when the two polar nuclei fuse to form the diploid central cell nucleus. Publication Abstract from PubMed The production of high-quality crystals is a key step in crystallography in general, but control of crystallization conditions is even more crucial in serial crystallography, which requires sets of crystals homogeneous in size and diffraction properties. This protocol describes the implementation of a simple and user-friendly microfluidic device that allows both the production of crystals by the counter-diffusion method and their in situ analysis by serial crystallography. As an illustration, the whole procedure is used to determine the crystal structure of three proteins from data collected at room temperature at a synchrotron radiation source. Protein crystallization and structure determination at room temperature in the CrystalChip.,Pachl P, Coudray L, Vincent R, Nilles L, Scheer H, Ritzenthaler C, Fejfarova A, Rezacova P, Engilberge S, Sauter C FEBS Open Bio. 2024 Nov 21. doi: 10.1002/2211-5463.13932. PMID:39572886 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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