7P4W

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

Summary for 7P4W

• Entry DOI: 10.2210/pdb7p4w/pdb
• Descriptor: Alpha-amylase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: amylase, aspergillus, oryzae, alpha-amylase, hydrolase
• Biological source: Aspergillus oryzae (Yellow koji mold)
• Total number of polymer chains: 1
• Total formula weight: 53011.53

Authors

Bellini, D.,Gorrec, F. (deposition date: 2021-07-13, release date: 2021-08-25, Last modification date: 2024-01-31)

Primary citation

Gorrec, F.,Bellini, D.
The FUSION protein crystallization screen.
J.Appl.Crystallogr., 55:310-319, 2022

PubMed Abstract: 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 α-amylase and avidin were discovered.

PubMed: 35497656
DOI: 10.1107/S1600576722001765

Experimental method

X-RAY DIFFRACTION (2.28 Å)