PDBsum entry 6hu5

Hydrolase

PDB id: 6hu5

Contents

Protein chains

129 a.a.

Metals

_CL ×3

PDB id:

6hu5

Name:

Hydrolase

Title:

Structure of hewl by electron diffraction and microfocus diffraction

Structure:

LysozymE C. Chain: a, b. Synonym: 1,4-beta-n-acetylmuramidasE C,allergen gal d iv. Ec: 3.2.1.17

Source:

Gallus gallus. Chicken. Organism_taxid: 9031

Authors:

G.Garau

Key ref:

A.Lanza et al. (2019). Nanobeam precession-assisted 3D electron diffraction reveals a new polymorph of hen egg-white lysozyme. IUCrJ, 6, 178-188. PubMed id: 30867915 DOI: 10.1107/S2052252518017657

Date:

05-Oct-18 Release date: 23-Jan-19

Protein chains

P00698  (LYSC_CHICK) -  Lysozyme C from Gallus gallus

Seq: 147 a.a.

Struc: 129 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.17 - lysozyme.
• Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

DOI no: 10.1107/S2052252518017657

IUCrJ 6:178-188 (2019)

PubMed id: 30867915

Nanobeam precession-assisted 3D electron diffraction reveals a new polymorph of hen egg-white lysozyme.

A.Lanza, E.Margheritis, E.Mugnaioli, V.Cappello, G.Garau, M.Gemmi.

ABSTRACT

Recent advances in 3D electron diffraction have allowed the structure determination of several model proteins from submicrometric crystals, the unit-cell parameters and structures of which could be immediately validated by known models previously obtained by X-ray crystallography. Here, the first new protein structure determined by 3D electron diffraction data is presented: a previously unobserved polymorph of hen egg-white lysozyme. This form, with unit-cell parameters a = 31.9, b = 54.4, c = 71.8 Å, β = 98.8°, grows as needle-shaped submicrometric crystals simply by vapor diffusion starting from previously reported crystallization conditions. Remarkably, the data were collected using a low-dose stepwise experimental setup consisting of a precession-assisted nanobeam of ∼150 nm, which has never previously been applied for solving protein structures. The crystal structure was additionally validated using X-ray synchrotron-radiation sources by both powder diffraction and single-crystal micro-diffraction. 3D electron diffraction can be used for the structural characterization of submicrometric macromolecular crystals and is able to identify novel protein polymorphs that are hardly visible in conventional X-ray diffraction experiments. Additionally, the analysis, which was performed on both nanocrystals and microcrystals from the same crystallization drop, suggests that an integrated view from 3D electron diffraction and X-ray microfocus diffraction can be applied to obtain insights into the molecular dynamics during protein crystal growth.