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Open data
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Basic information
Entry | Database: PDB / ID: 194l | ||||||
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Title | THE 1.40 A STRUCTURE OF SPACEHAB-01 HEN EGG WHITE LYSOZYME | ||||||
![]() | 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. / Maignan, S. / Ries-Kautt, M. / Ducruix, A. | ||||||
![]() | ![]() Title: High-resolution structure (1.33 A) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission. Authors: Vaney, M.C. / Maignan, S. / Ries-Kautt, M. / Ducriux, A. #1: ![]() Title: Effect of Microgravity on Rate of Nucleation, Size and Quality of Lysozyme Crystals Grown in the Advanced Protein Crystallization Facility on Spacehab-01 Authors: Ries-Kautt, M.M. / Broutin, I. / Ducruix, A.F. / Shephard, W. / Kahn, R. / Lorber, B. / Theobald, A. / Giege, R. / Chayen, N. / Blow, D. / Paal, K. / Littke, W. #2: ![]() Title: Thermal Expansion of Hen-Egg-White Lysozyme. Comparison of the 1.9 Angstroms Resolution Structures of the Tetragonal Form of the Enzyme at 100K and 298K Authors: Young, A.C.M. / Tilton, R.F. / Dewan, J.C. #3: ![]() Title: Experiment Equipment for Protein Crystallization in Micro-Grammes Facilities Authors: Bosch, R. / Lautenschlager, P. / Potthast, L. / Stapelmann, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 37.1 KB | Display | ![]() |
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PDB format | ![]() | 28.4 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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1 |
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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-CL / |
#3: Chemical | ChemComp-NA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.62 % | ||||||||||||||||||||||||
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Crystal grow | pH: 4.3 / Details: pH 4.3 | ||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 1, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.901 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→15 Å / Num. obs: 21542 / % possible obs: 90.2 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.027 |
Reflection | *PLUS Rmerge(I) obs: 0.027 / Biso Wilson estimate: 17.4 Å2 |
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Processing
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Refinement | Resolution: 1.4→7 Å / σ(F): 0 Details: SOME OF THE SIDE CHAIN ATOMS OF RESIDUES ARG 21, TRP 62, ARG 73, ASN 77, LYS 97, ASN 103, ASP 119, GLN 121, ARG 125, ARG 128, AND LEU 129 HAVE A POORLY DEFINED DENSITY. THESE ATOMS WERE ...Details: SOME OF THE SIDE CHAIN ATOMS OF RESIDUES ARG 21, TRP 62, ARG 73, ASN 77, LYS 97, ASN 103, ASP 119, GLN 121, ARG 125, ARG 128, AND LEU 129 HAVE A POORLY DEFINED DENSITY. THESE ATOMS WERE BUILT USING STEREOCHEMICAL CONSTRAINTS AND KEPT IN THE COORDINATE FILE. ALTERNATE CONFORMATIONS WERE MODELED FOR RESIDUES LYS 1, SER 86 AND VAL 109. THE OCCUPANCY FACTORS WERE REFINED FOR THESE RESIDUES. WATER MOLECULES 268 AND 269 ARE ON A TWO-FOLD AXIS AND HAVE BEEN MODELED WITH 50% OCCUPANCY.
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Displacement parameters | Biso mean: 21.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.15 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.4→7 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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