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Open data
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Basic information
Entry | Database: PDB / ID: 1i5i | ||||||
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Title | THE C18S MUTANT OF BOVINE (GAMMA-B)-CRYSTALLIN | ||||||
![]() | (GAMMA-B) CRYSTALLIN | ||||||
![]() | STRUCTURAL PROTEIN / EYE LENS PROTEIN / CRYSTALLIN | ||||||
Function / homology | ![]() structural constituent of eye lens / lens development in camera-type eye / visual perception Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Zarutskie, J.A. / Asherie, N. / Pande, J. / Pande, A. / Lomakin, J. / Lomakin, A. / Ogun, O. / Stern, L.J. / King, J.A. / Benedek, G.B. | ||||||
![]() | ![]() Title: Enhanced crystallization of the Cys18 to Ser mutant of bovine gammaB crystallin. Authors: Asherie, N. / Pande, J. / Pande, A. / Zarutskie, J.A. / Lomakin, J. / Lomakin, A. / Ogun, O. / Stern, L.J. / King, J. / Benedek, G.B. #1: ![]() Title: Structure of the Bovine Eye Lens Protein Gamma-B (Gamma-II)-Crystallin at 1.47 Angstroms Authors: Najmudin, S. / Nalini, V. / Driessen, H.P.C. / Slingsby, C. / Blundell, T.L. / Moss, D.S. / Lindley, P.F. #2: ![]() Title: X-Ray Studies of the Lens Specific Proteins, the Crystallins Authors: Summers, L. / Wistow, G. / Narebor, M. / Moss, D. / Lindley, P. / Slingsby, C. / Blundell, T. / Bartunik, H. / Bartels, K. #3: ![]() Title: X-ray analysis of the eye lens protein Gamma-II Crystallin at 1.9 Angstrom Resolution Authors: Wistow, G. / Turnell, B. / Summers, L. / Slingsby, C. / Moss, D. / Miller, L. / Lindley, P. / Blundell, T. #4: ![]() Title: The molecular structure and stability of the eye lens: X-Ray Analysis of Gamma-Crystallin II Authors: Blundell, T. / Lindley, P. / Miller, L. / Moss, D. / Slingsby, C. / Tickle, I. / Turnell, B. / Wistow, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 50.1 KB | Display | ![]() |
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PDB format | ![]() | 35.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 427.5 KB | Display | ![]() |
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Full document | ![]() | 430.3 KB | Display | |
Data in XML | ![]() | 9.6 KB | Display | |
Data in CIF | ![]() | 12.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4gcrS S: Starting model for refinement |
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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: 20976.494 Da / Num. of mol.: 1 / Mutation: C18S 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: 1.97 Å3/Da / Density % sol: 37.49 % |
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Crystal grow | Temperature: 295 K Method: chill tube containing protein to 265 k, then bring to 295 k pH: 7 Details: 100 mM Phosphate, 20 mM DTT, pH 7.0, chill tube containing protein to 265 K, then bring to 295 K |
-Data collection
Diffraction | Mean temperature: 296 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Jun 26, 1999 / Details: MIRRORS |
Radiation | Monochromator: Ni Filter / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→20 Å / Num. obs: 6843 / % possible obs: 97.1 % / Observed criterion σ(I): 2 / Redundancy: 10 % / Biso Wilson estimate: 28 Å2 / Rmerge(I) obs: 0.074 / Rsym value: 0.074 / Net I/σ(I): 21.6 |
Reflection shell | Resolution: 2.4→2.44 Å / Redundancy: 7.5 % / Rmerge(I) obs: 0.146 / Mean I/σ(I) obs: 9.6 / Num. unique all: 6843 / Rsym value: 0.146 / % possible all: 92.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4GCR Resolution: 2.4→20 Å / Rfactor Rfree error: 0.009 / Data cutoff high absF: 100000 / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 2 / Stereochemistry target values: Engh & Huber Details: Due to weak electron density in the region of the Tyrosine 174, a good model for the residue could not be refined, and is thus not included in the structure. Density was weak for the CG, SD, ...Details: Due to weak electron density in the region of the Tyrosine 174, a good model for the residue could not be refined, and is thus not included in the structure. Density was weak for the CG, SD, and CE of MET 160 and was not included in the structure.
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Displacement parameters | Biso mean: 13.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.4→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.55 Å / Rfactor Rfree error: 0.023 / Total num. of bins used: 6
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