+Open data
-Basic information
Entry | Database: PDB / ID: 1msp | ||||||
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Title | MAJOR SPERM PROTEIN, ALPHA ISOFORM (RECOMBINANT), PH 4.6 | ||||||
Components | MAJOR SPERM PROTEIN | ||||||
Keywords | CELL MOTILITY PROTEIN / CYTOSKELETAL PROTEIN / SPERM | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Ascaris suum (pig roundworm) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Bullock, T.L. / Roberts, T.M. / Stewart, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1996 Title: 2.5 A resolution crystal structure of the motile major sperm protein (MSP) of Ascaris suum. Authors: Bullock, T.L. / Roberts, T.M. / Stewart, M. #1: Journal: Cell(Cambridge,Mass.) / Year: 1996 Title: Worm Sperm and Advances in Cell Locomotion Authors: Theriot, J.A. #2: Journal: J.Struct.Biol. / Year: 1996 Title: New Crystal Forms of the Motile Major Sperm Protein (Msp) of Ascaris Suum Authors: Bullock, T.L. / Parthasarathy, G. / King, K.L. / Kent, H.M. / Roberts, T.M. / Stewart, M. #3: Journal: Curr.Opin.Cell Biol. / Year: 1995 Title: Nematode Sperm Locomotion Authors: Roberts, T.M. / Stewart, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1msp.cif.gz | 60.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1msp.ent.gz | 44.2 KB | Display | PDB format |
PDBx/mmJSON format | 1msp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ms/1msp ftp://data.pdbj.org/pub/pdb/validation_reports/ms/1msp | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14278.107 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: ALPHA ISOFORM, PH 4.6 / Source: (gene. exp.) Ascaris suum (pig roundworm) / Cell: SPERM CELL / Gene: ALPHA MSP / Plasmid: PET11D / Species (production host): Escherichia coli / Gene (production host): ALPHA MSP / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P27439 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||
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Crystal grow | pH: 4.6 / Details: pH 4.6 | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 8858 / % possible obs: 95 % / Observed criterion σ(I): 0 / Redundancy: 1.9 % / Rmerge(I) obs: 0.046 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 21 Å |
-Processing
Software |
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Refinement | Resolution: 2.5→20 Å / Num. reflection obs: 8478 / σ(F): 0 / Stereochemistry target values: TNT | ||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 21 Å / % reflection Rfree: 5 % / Rfactor obs: 0.195 / Rfactor Rfree: 0.292 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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