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- PDB-1b0d: Structural effects of monovalent anions on polymorphic lysozyme c... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1b0d | ||||||
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Title | Structural effects of monovalent anions on polymorphic lysozyme crystals | ||||||
![]() | LYSOZYME | ||||||
![]() | HYDROLASE / O-GLYCOSYL | ||||||
Function / homology | ![]() 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 | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Vaney, M.C. / Broutin, I. / Retailleau, P. / Lafont, S. / Hamiaux, C. / Prange, T. / Ries-Kautt, M. / Ducruix, A. | ||||||
![]() | ![]() Title: Structural effects of monovalent anions on polymorphic lysozyme crystals. Authors: Vaney, M.C. / Broutin, I. / Retailleau, P. / Douangamath, A. / Lafont, S. / Hamiaux, C. / Prange, T. / Ducruix, A. / Ries-Kautt, M. #1: ![]() Title: Refinement of Triclinic Hen Egg-White Lysozyme at Atomic Resolution Authors: Walsh, M.A. / Schneider, T.R. / Sieker, L.C. / Dauter, Z. / Lamzin, V.S. / Wilson, K.S. #2: ![]() Title: Structures of Monoclinic Lysozyme Iodide at 1.6 Ang. and of Triclinic Lysozyme Nitrate at 1.1 Ang Authors: Steinrauf, L.K. #3: ![]() Title: Locations of Bromide Ions in Tetragonal Lysozyme Crystals Authors: Lim, K. / Nadarajah, A. / Forsythe, E.L. / Pusey, M.L. #4: ![]() Title: High-Resolution Structure (1.33 Ang.) Of a Hewl Lysozyme Tetragonal Crystal Grown in the Apcf Apparatus. Data and Structural Comparison with a Crystal Grown Under Microgravity from Spachab-01 Mission Authors: Vaney, M.C. / Maignan, S. / Ries-Kautt, M. / Ducruix, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 39.5 KB | Display | ![]() |
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PDB format | ![]() | 27 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 14331.160 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Chemical | ChemComp-TSU / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 40.58 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: THE CRYSTAL WAS OBTAINED IN PRESENCE OF NAPTS WITH A FINAL PROTEIN CONCENTRATION OF 40.5 MG/ML IN HANGING DROPS USING VAPOR DIFFUSION METHOD. THE EQUILIBRATION AT 291K WAS DONE AGAINST A ...Details: THE CRYSTAL WAS OBTAINED IN PRESENCE OF NAPTS WITH A FINAL PROTEIN CONCENTRATION OF 40.5 MG/ML IN HANGING DROPS USING VAPOR DIFFUSION METHOD. THE EQUILIBRATION AT 291K WAS DONE AGAINST A RESERVOIR SOLUTION CONTAINING 90 MM NAPTS, 50 MM SODIUM ACETATE ADJUSTED AT PH 4.5., vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 291 K / Method: vapor diffusion, hanging dropDetails: drop consists of equal volume of protein and reservoir solutions | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Apr 1, 1994 |
Radiation | Protocol: MONOCHROMATIC / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→13.5 Å / Num. obs: 10462 / % possible obs: 97.5 % / Observed criterion σ(I): 0 / Redundancy: 6.6 % / Biso Wilson estimate: 21.4 Å2 / Rsym value: 0.049 / Net I/σ(I): 10.5 |
Reflection shell | Resolution: 1.85→1.9 Å / Redundancy: 4.1 % / Mean I/σ(I) obs: 4.5 / Rsym value: 0.135 / % possible all: 85.8 |
Reflection | *PLUS Num. obs: 10484 / Rmerge(I) obs: 0.049 |
Reflection shell | *PLUS % possible obs: 85.8 % / Rmerge(I) obs: 0.135 |
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Processing
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Refinement | Method to determine structure: OTHER / Resolution: 1.84→14 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: SOME OF THE SIDE CHAIN ATOMS OF RESIDUES ARG 61, ARG 73, ASN 77, LYS 97, ASP 101, ASN 103, GLN 121 AND ARG 125 HAVE A POORLY DEFINED DENSITY. THESE ATOMS WERE BUILT USING STEREOCHEMICAL ...Details: SOME OF THE SIDE CHAIN ATOMS OF RESIDUES ARG 61, ARG 73, ASN 77, LYS 97, ASP 101, ASN 103, GLN 121 AND ARG 125 HAVE A POORLY DEFINED DENSITY. THESE ATOMS WERE BUILT USING STEREOCHEMICAL CONSTRAINTS AND KEPT IN THE COORDINATE FILE.
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Displacement parameters | Biso mean: 18.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.84→14 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.84→1.92 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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