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. Author manuscript; available in PMC: 2013 Nov 1.
Published in final edited form as: Sens Actuators B Chem. 2012 Nov;174:1–9. doi: 10.1016/j.snb.2012.08.048

Table 2.

Crystallographic data statistics from the analysis of lysozyme crystals.

Parameter On-Chipa Traditional (Cryogenic)b
Unit Cell Dimensions a = b = 79.693Å
c = 37.781Å
a = b = 78.817Å
c = 37.025Å
Space Group P43212 P43212
Observations (Unique) 783,994 (18,352) 223,433 (17,510)
Resolution 50 – 1.55Å 50 – 1.55Å
Rsym 0.064 (0.362) 0.052 (0.102)
Mosaicity 0.03° – 0.08° 0.21° – 0.34°
Redundancy 22.9 (5.7) 7.7 (7.7)
Completeness 98.1% (83.4%) 99.7% (100%)
I/σ 51.4 (3.9) 42.3 (19.4)
# of Frames 363 100

Refinement
R (Rfree) 0.164 (0.227) 0.173 (0.276)

Ramachandran Statistics
Most Favored 96.1% (122) 96.1% (122)
Allowed 3.9% (5) 3.9% (5)
Disallowed 0.0% (0) 0.0% (0)
a

Merging of small datasets from "multiple crystals" analyzed on-chip within a 24-well device at room temperature.

b

The "traditional" sample was grown using microbatch techniques and mounted using a standard crystal mount for cryogenic data collection. Reported values are for all hkls. Values in parenthesis represent the value for the highest resolution shell except where indicated for the number of observations as compared to unique reflections and R (Rfree) and for the Ramachandran statistics here the number in parenthesis indicates the number of residues in a given region. Data was analyzed over the range of 50 – 1.55Å to enable a direct comparison with the data collected from merging the diffraction data taken from multiple crystals at RT.