7p4w | pdb_00007p4w

Crystal structure of alpha-amylase from Aspergillus oryzae in space group I222

spinqualitylabelsall models 7p4w, resolution 2.28Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7p4w is a 1 chain structure with sequence from Aspergillus oryzae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.28Å Ligands: CA, MES, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AMYA1_ASPOR Publication Abstract from PubMed The success and speed of atomic structure determination of biological macromolecules by X-ray crystallography depends critically on the availability of diffraction-quality crystals. However, the process of screening crystallization conditions often consumes large amounts of sample and time. An innovative protein crystallization screen formulation called FUSION has been developed to help with the production of useful crystals. The concept behind the formulation of FUSION was to combine the most efficient components from the three MORPHEUS screens into a single screen using a systematic approach. The resulting formulation integrates 96 unique combinations of crystallization additives. Most of these additives are small molecules and ions frequently found in crystal structures of the Protein Data Bank (PDB), where they bind proteins and complexes. The efficiency of FUSION is demonstrated by obtaining high yields of diffraction-quality crystals for seven different test proteins. In the process, two crystal forms not currently in the PDB for the proteins alpha-amylase and avidin were discovered. The FUSION protein crystallization screen.,Gorrec F, Bellini D J Appl Crystallogr. 2022 Mar 11;55(Pt 2):310-319. doi: 10.1107/S1600576722001765., eCollection 2022 Apr 1. PMID:35497656 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Amylase 3D structures

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