2YGY

Structure of wild type E. coli N-acetylneuraminic acid lyase in space group P21 crystal form II

Summary for 2YGY

• Entry DOI: 10.2210/pdb2ygy/pdb
• Related: 1FDY 1FDZ 1HL2 1NAL 2WKJ 2WNN 2WNQ 2WNZ 2WO5 2WPB 2XFW 2YGZ
• Descriptor: N-ACETYLNEURAMINATE LYASE, CHLORIDE ION, PENTAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: lyase, directed evolution, substrate specificity, protein engineering
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 4
• Total formula weight: 134955.84

Authors

Campeotto, I.,Nelson, A.,Berry, A.,Phillips, S.E.V.,Pearson, A.R. (deposition date: 2011-04-23, release date: 2012-04-04, Last modification date: 2023-12-20)

Primary citation

Campeotto, I.,Lebedev, A.,Schreurs, A.M.M.,Kroon-Batenburg, L.M.J.,Lowe, E.,Phillips, S.E.V.,Murshudov, G.N.,Pearson, A.R.
Pathological macromolecular crystallographic data affected by twinning, partial-disorder and exhibiting multiple lattices for testing of data processing and refinement tools.
Sci Rep, 8:14876-14876, 2018

PubMed Abstract: Twinning is a crystal growth anomaly, which has posed a challenge in macromolecular crystallography (MX) since the earliest days. Many approaches have been used to treat twinned data in order to extract structural information. However, in most cases it is usually simpler to rescreen for new crystallization conditions that yield an untwinned crystal form or, if possible, collect data from non-twinned parts of the crystal. Here, we report 11 structures of engineered variants of the E. coli enzyme N-acetyl-neuraminic lyase which, despite twinning and incommensurate modulation, have been successfully indexed, solved and deposited. These structures span a resolution range of 1.45-2.30 Å, which is unusually high for datasets presenting such lattice disorders in MX and therefore these data provide an excellent test set for improving and challenging MX data processing programs.

PubMed: 30291262
DOI: 10.1038/s41598-018-32962-6

Experimental method

X-RAY DIFFRACTION (1.9 Å)