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- PDB-8rlh: Neutron structure of hydrogenated hen egg-white lysozyme at room ... -

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Basic information

Entry
Database: PDB / ID: 8rlh
TitleNeutron structure of hydrogenated hen egg-white lysozyme at room temperature
ComponentsLysozyme C
KeywordsHYDROLASE / lysozyme / hydrogenated / room temperature
Function / homology
Function and homology information


Lactose synthesis / Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium ...Lactose synthesis / Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium / defense response to bacterium / endoplasmic reticulum / extracellular space / identical protein binding / cytoplasm
Similarity search - Function
Glycoside hydrolase, family 22, lysozyme / Glycoside hydrolase family 22 domain / Glycosyl hydrolases family 22 (GH22) domain signature. / Glycoside hydrolase, family 22 / C-type lysozyme/alpha-lactalbumin family / Glycosyl hydrolases family 22 (GH22) domain profile. / Alpha-lactalbumin / lysozyme C / Lysozyme-like domain superfamily
Similarity search - Domain/homology
ACETATE ION / DEUTERATED WATER / NITRATE ION / Lysozyme C
Similarity search - Component
Biological speciesGallus gallus (chicken)
MethodNEUTRON DIFFRACTION / NUCLEAR REACTOR / MOLECULAR REPLACEMENT / Resolution: 1.1 Å
AuthorsRamos, J. / Laux, V. / Mason, S.A. / Lemee, M. / Bowler, M. / Diederichs, K. / Haertlein, M. / Forsyth, V.T. / Mossou, E. / Larsen, S. / Langkilde, A.E.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Structure / Year: 2025
Title: Structure and dynamics of the active site of hen egg-white lysozyme from atomic resolution neutron crystallography.
Authors: Ramos, J. / Laux, V. / Mason, S.A. / Lemee, M.H. / Bowler, M.W. / Diederichs, K. / Haertlein, M. / Forsyth, V.T. / Mossou, E. / Larsen, S. / Langkilde, A.E.
History
DepositionJan 3, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 6, 2024Provider: repository / Type: Initial release
Revision 1.1Jan 29, 2025Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Lysozyme C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,94811
Polymers14,3311
Non-polymers61710
Water1,892105
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11360 Å2
ΔGint40 kcal/mol
Surface area9130 Å2
MethodPISA
Unit cell
Length a, b, c (Å)27.290, 31.940, 34.350
Angle α, β, γ (deg.)88.64, 71.51, 68.17
Int Tables number1
Space group name H-MP1

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Components

#1: Protein Lysozyme C / 1 / 4-beta-N-acetylmuramidase C / Allergen Gal d IV


Mass: 14331.160 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / References: UniProt: P00698, lysozyme
#2: Chemical
ChemComp-NO3 / NITRATE ION


Mass: 62.005 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: NO3
#3: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H3O2
#4: Chemical ChemComp-DOD / water


Mass: 18.015 Da / Num. of mol.: 105 / Source method: isolated from a natural source / Formula: D2O
Has ligand of interestN
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: NEUTRON DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal growTemperature: 291 K / Method: batch mode / pH: 4.5 / Details: 2 % NaNO3, 0.1 M Na acetate pH 4.5

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Data collection

DiffractionMean temperature: 298 K / Serial crystal experiment: N
Diffraction sourceSource: NUCLEAR REACTOR / Site: ILL / Beamline: D19 / Wavelength: 1.458 Å
DetectorType: 5ATM 3HE, CURVED 120X30 DEGREES / Detector: POSITION SENSITIVE DETECTOR / Date: Sep 10, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: neutron
Radiation wavelengthWavelength: 1.458 Å / Relative weight: 1
ReflectionResolution: 1.1→9.96 Å / Num. obs: 38932 / % possible obs: 94.5 % / Redundancy: 2.2 % / CC1/2: 0.993 / Rmerge(I) obs: 0.089 / Rpim(I) all: 0.056 / Rrim(I) all: 0.107 / Net I/σ(I): 5.7
Reflection shellResolution: 1.1→1.14 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.585 / Mean I/σ(I) obs: 1.5 / Num. unique obs: 3703 / CC1/2: 0.545 / Rpim(I) all: 0.494 / Rrim(I) all: 0.769 / % possible all: 88.8

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Processing

RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.1→9.96 Å / Cross valid method: FREE R-VALUE
RfactorNum. reflection% reflectionSelection details
Rfree0.2343 1947 5.2 %Random
Rwork0.186 ---
obs-36985 94.5 %-

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