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1NO7

Structure of the Large Protease Resistant Upper Domain of VP5, the Major Capsid Protein of Herpes Simplex Virus-1

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-BM
Synchrotron siteAPS
Beamline19-BM
Temperature [K]100
Detector technologyCCD
Collection date2000-12-21
DetectorCUSTOM-MADE
Wavelength(s).97885
Spacegroup nameP 41 21 2
Unit cell lengths99.072, 99.072, 454.684
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution50.000

*

- 2.900
R-factor0.255
Rwork0.255
R-free0.28900
Structure solution methodMAD
RMSD bond length0.013
RMSD bond angle23.000

*

Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.000
High resolution limit [Å]2.9002.900
Rmerge0.101

*

0.205

*

Total number of observations308549

*

Number of reflections47194
<I/σ(I)>73.3
Completeness [%]91.280.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

8

*

4

*

sodium acetate, imidazole, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K
1Vapor diffusion

*

8

*

4

*

sodium acetate, imidazole, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11drop250 (mM)
21dropTris10 (mM)pH8.0
31dropdithiothreitol10 (mM)
41dropprotein20 (mg/ml)
51reservoirsodium acetate0.8-1 (M)
61reservoirimidizole100 (mM)pH6.0-6.8

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PDB entries from 2024-09-11

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