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Table 1 Data collection and refinement statistics.

From: Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx

Data collection    
   Beamline DESY X12
   Temperature (K) 100
   Dataset type Peak Inflection point High-energy remote
   Wavelength (Å) 1.10371 1.10420 1.10009
   Data range (°) 180
   Oscillation range (°) 0.5
   Space group P31
   Unit cell parameters (Å) a = b = 53.0, c = 143.5
   Resolution (Å) 20 to 2.8 (2.95 to 2.8)
   Unique reflections 19,800 (3,352) 19,790 (3,392) 19,765 (3,365)
   Redundancy 2.84 (2.84) 2.83 (2.82) 2.84 (2.84)
   Completeness (%) 90.0 (94.5) 89.9 (96.9) 89.7 (95.9)
   Mean I/σI 16.5 (3.45) 15.52 (2.92) 18.19 (3.84)
   Rmergea 0.05 (0.30) 0.06 (0.40) 0.05 (0.28)
   Mosaicity (°) 0.271
   Estimated Wilson B2) 54.1
Refinement    
   R work b 0.2271
   R free c 0.2508
Molecules in the asymmetric unit
(DC-LAMP/GlcNAc/Ir)
2/2/4
   No. of atoms    
Protein 2,438
Hetero atoms 32
Water 10
Total 2,480
   Atomic displacement factor B2) 61.3
   Real space correlation coefficientd 0.882
   r.m.s.d. from ideal    
Bond lengths (Å) 0.0056
Bond angles (°) 1.023
   Ramachandran plot    
Favored (%) 90.9
Allowed (%) 6.8
Disallowed (%) 2.3
  1. Values in parentheses account for the highest resolution shell.
  2. a R m e r g e = h k l i I h k l , i - I h k l ¯ h k l i I h k l , i
  3. b R w o r k = h k l F o b s - F c a l c h k l F o b s
  4. c R free is calculated as R work but using F obs derived from 5% randomly selected reflections exclude from refinement.
  5. d R S C C = x y z ρ o - ρ o ¯ x y z ρ c - ρ c ¯ / x y z ρ o - ρ o ¯ 2 x y z ρ c - ρ c ¯ 2 1 / 2