ISDA: 9WKS

Deposition Date 2025-09-01

Release Date 2026-03-11

Last Version Date 2026-03-11

Entry Detail

PDB ID:

9WKS

Keywords:

HYDROLASE

Title:

Crystal structure of hen egg-white lysozyme determined in the commissioning of NanoTerasu MX-ES

Biological Source:

Source Organism(s):

Gallus gallus (Taxon ID: 9031)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

1.20 Å

R-Value Free:

0.17

R-Value Work:

0.14

R-Value Observed:

0.14

Space Group:

P 43 21 2

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Lysozyme C
Gene (Uniprot):LYZ
Chain IDs:A
Chain Length:129
Number of Molecules:1
Biological Source:Gallus gallus

UniProt ID:P00698 Pfam ID:PF00062 EC:3.2.1.17

Ligand Molecules

Primary Citation

A new macromolecular crystallography endstation at NanoTerasu for accelerating structural biology and drug discovery.

Yamada, Y, Sakurai, K, Fukuda, A, Yamane, H, Hatano, T, Nakamura, T, Ueno, G, Masunaga, T, Yamamoto, M, Nango, E.Show

Acta Crystallogr D Struct Biol 82 23 29 (2026)

PMID: 41420545 DOI: 10.1107/S2059798325011234

Abstact

Since the fiscal year 2022, ;Support Program for Life Science and Drug Discovery Research (BINDS Phase II)', funded by the Japan Agency for Medical Research and Development (AMED), has been supporting structural analysis research in Japan, promoting the further development of various advanced structural analysis technologies. The BINDS project aims to offer more timely and cutting-edge support by establishing a new macromolecular crystallography endstation (MX-ES) at NanoTerasu, Japan's first fourth-generation synchrotron-radiation facility. MX-ES has been equipped with microbeam focusing optics and a state-of-the-art measurement system for fully automated, high-throughput data collection from cooled crystals. Commissioning and initial experiments have been completed. User operations are expected to begin in the second half of the fiscal year 2025.

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Primary Citation of related structures

Abstact

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