Skip to main content

Table 1 X-ray data collection and refinement statistics of OxyR (NMB0173)

From: The structure of a reduced form of OxyR from Neisseria meningitidis

Data collection details:   
   X-ray source ESRF BM14  
   Data set Peak remote
   Wavelength (Å) 0.9785 0.9070
   Space group P2 1  
   Unit cell (Å) a = 49.81, b = 56.08, c = 81.25, β = 104.9°  
   Resolution range (Å) 30.0 - 2.40 (2.49 - 2.40)  
   Unique reflections 16661(1280) 16617(1122)
   Completenessa (%) 96.8(76.1) 95.1(65.4)
   Redundancy 6.9(4.6) 3.9(2.8)
   Average I(/σI) 18.4(2.6) 12.7(2.0)
   Rmerge 0.129(0.554) 0.113(0.547)
Refinement statistics:   
   Resolution range (Å) 30.0 - 2.40 (2.49 - 2.40)  
   No. of reflections (working/test) 32077/1617  
   R-factorb(Rwork/Rfree) 0.218/0.294  
   No. of atoms (protein/water) 3254/98  
   Rms bond length deviation (Å) 0.009  
   Rms bond angle deviation (°) 1.3  
   Mean B-factor (protein/water[Å2]) 55.7/54.3  
Ramachandran plot:   
Most favoured regions (%) 85.5  
Allowed regions (%) 15.5  
Disallowed regions(%) 0  
  1. a The data are essentially complete to 2.6 Å resolution.
  2. b Rwork and Rfree are defined by R = Σhkl||F obs |-|F calc ||/Σhkl|F obs |, where h,k,l are the indices of the reflections (used in refinement for Rwork; 5%, not used in refinement, for Rfree), F obs and F calc are the structure factors, deduced from measured intensities and calculated from the model, respectively.