9EAT

High-Resolution Structure of Escherichia coli Carbonic Anhydrase 2 in Space Group P4(2)2(1)2

Summary for 9EAT

Entry DOI	10.2210/pdb9eat/pdb
Descriptor	Carbonic anhydrase 2, ZINC ION (3 entities in total)
Functional Keywords	zinc-dependent metalloenzyme, lyase
Biological source	Escherichia coli BL21(DE3)
Total number of polymer chains	1
Total formula weight	25196.19
Authors	Rankin, M.R.,Smith, J.L. (deposition date: 2024-11-11, release date: 2024-11-20, Last modification date: 2025-02-12)
Primary citation	Rankin, M.R.,Smith, J.L. Serendipitous high-resolution structure of Escherichia coli carbonic anhydrase 2. Acta Crystallogr.,Sect.F, 81:47-52, 2025 Cited by PubMed Abstract: X-ray crystallography remains the dominant method of determining the three-dimensional structure of proteins. Nevertheless, this resource-intensive process may be hindered by the unintended crystallization of contaminant proteins from the expression source. Here, the serendipitous discovery of two novel crystal forms and one new, high-resolution structure of carbonic anhydrase 2 (CA2) from Escherichia coli that arose during a crystallization campaign for an unrelated target is reported. By comparing unit-cell parameters with those in the PDB, contaminants such as CA2 can be identified, preventing futile molecular-replacement attempts. Crystallographers can use these new lattice parameters to diagnose CA2 contamination in similar experiments. PubMed: 39812168 DOI: 10.1107/S2053230X25000068 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.43 Å)

Structure validation