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Open data
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Basic information
Entry | Database: PDB / ID: 2f4g | ||||||
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Title | Triclinic cross-linked lysozyme soaked in bromoethanol 1M | ||||||
![]() | Lysozyme C | ||||||
![]() | HYDROLASE / DENATURATION / LYSOZYME / BARNASE / CROSS-LINKED CRYSTALS / GLUTARALDEHYDE / UREA / THIOUREA / BROMOETHANOL | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Prange, T. / Salem, M. | ||||||
![]() | ![]() Title: On the edge of the denaturation process: Application of X-ray diffraction to barnase and lysozyme cross-linked crystals with denaturants in molar concentrations. Authors: Salem, M. / Mauguen, Y. / Prange, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 40.4 KB | Display | ![]() |
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PDB format | ![]() | 26.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2f2nSC ![]() 2f30C ![]() 2f4aC ![]() 2f4yC ![]() 2f56C ![]() 2f5mC ![]() 2f5wC S: Starting model for refinement C: citing same article ( |
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Similar 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
#1: Protein | Mass: 14331.160 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: EGG / Source: (natural) ![]() ![]() | ||||
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#2: Chemical | #3: Chemical | ChemComp-BRJ / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.81 Å3/Da / Density % sol: 31.78 % |
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Crystal grow | Temperature: 300 K / Method: vapor diffusion, hanging drop / pH: 6 Details: SODIUM NITRATE AS CRYSTALLIZING AGENT CROSS-LINKED BY VAPOR DIFFUSION WITH GLUTARALDEHYDE, PROTEIN 20 MG/ML, pH 6.00, VAPOR DIFFUSION, HANGING DROP, temperature 300K |
-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 13, 2002 / Details: SI(111) CURVATED MIRROR |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.964 Å / Relative weight: 1 |
Reflection | Resolution: 1.654→10 Å / Num. all: 11237 / Num. obs: 10770 / % possible obs: 90.1 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 4 |
Reflection shell | Resolution: 1.654→1.8 Å / % possible all: 90.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2F2N Resolution: 1.654→10 Å / Num. parameters: 4343 / Num. restraintsaints: 4170 / σ(F): 2 / σ(I): 4 / Stereochemistry target values: ENGH AND HUBER
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Refine analyze | Num. disordered residues: 0 / Occupancy sum hydrogen: 909 / Occupancy sum non hydrogen: 1085 | |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.654→10 Å
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Refine LS restraints |
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LS refinement shell |
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