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In this study the x-ray structure of bovine aquaporin 0 (AQP0) was determined …


Biology Articles » Biochemistry » The channel architecture of aquaporin 0 at a 2.2-Å resolution » Table

Table
- The channel architecture of aquaporin 0 at a 2.2-Å resolution

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Table 1. Crystallographic statistics of 2.2-Å data. Data were collected at ALS Beamline 8.3.1 with an 2 × 2 charge-coupled device detector (ADSC, Poway, CA), integrated, and scaled with mosflm/scala and denzo/scalepack (18, 20). Phasing calculations were carried out by using molecular replacement with bAQP1 as the model, and cns was used for the data refinement. The rms deviation from ideal geometry is given. Rsym = ∑hkli|Ihkl,ileft angle bracketIhkl,iright angle bracket|/∑hkli|Ihkl,i|, where left angle bracketIhkl,iright angle bracket is the average intensity of the multiple hkl observations for symmetry-related reflections. Rcryst = ∑|Fobs — Fcalc|∑Fobs, where Fobs and Fcalc are observed and calculated structure factors, respectively, Rfree is calculated from a randomly chosen 10% of reflections, and Rcryst is calculated over the remaining 90% of reflections.

Data collection statistics  
        Wavelength, Å 1.0
        Resolution, Å 30.0-2.2
        Total reflections 340,485
        Unique reflections 14,682
        Completeness, % (last shell)* 89.5 (49.2)
        Rsym, % (last shell) 4.1 (50.4)
        I/σ (last shell) 28.0 (2.6)
Refinement statistics  
        Space group P4212
        Unit cell dimensions a = 110.5, c = 53.4
        Resolution, Å 30.0-2.2
        Rcryst, % 24.8
        Rfree, % 27.1
        rms deviation bonds, Å 0.006
        rms deviation angles, Å 1.207
        Nonhydrogen protein atoms 1,803
        Nonhydrogen heteroatoms 42
        Solvent molecules 181
        Average B-factors, Å2 54.7
        B values from Wilson Plot, Å2 25.7
*Last-shell resolution, 2.28-2.20.

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Source: Proc Natl Acad Sci U S A. 2004 September 28; 101(39): 14045–14050. 


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