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- PDB-3lym: CRYSTAL STRUCTURE OF HEN EGG-WHITE LYSOZYME AT A HYDROSTATIC PRES... -
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Basic information
Entry | Database: PDB / ID: 3lym | ||||||
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Title | CRYSTAL STRUCTURE OF HEN EGG-WHITE LYSOZYME AT A HYDROSTATIC PRESSURE OF 1000 ATMOSPHERES | ||||||
![]() | HEN EGG WHITE 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 | ![]() | ||||||
![]() | Kundrot, C.E. / Richards, F.M. | ||||||
![]() | ![]() Title: Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres. Authors: Kundrot, C.E. / Richards, F.M. #1: ![]() Title: The Effect of Hydrostatic Pressure on the Solvent in Crystals of Hen Egg White Lysozyme Authors: Kundrot, C.E. / Richards, F.M. #2: ![]() Title: Collection and Processing of X-Ray Diffraction Data from Protein Crystals at High Pressure Authors: Kundrot, C.E. / Richards, F.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 36.4 KB | Display | ![]() |
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PDB format | ![]() | 28 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-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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Atom site foot note | 1: SEE REMARK 4. |
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Components
#1: Protein | Mass: 14331.160 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.05 Å3/Da / Density % sol: 40.06 % | ||||||||||||||||||
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Crystal grow | *PLUS pH: 4.7 / Method: unknown | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2 Å / Rmerge(I) obs: 0.124 |
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Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2→78.7 Å / Rfactor obs: 0.149 / σ(F): 0 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→78.7 Å
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