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. 1999 Aug 3;96(16):8949–8954. doi: 10.1073/pnas.96.16.8949

Table 3.

Crystallographic data for mutant lysozymes

Mutant E11H E11N D20E D20C T26D T26E (Apo) T26H T26Q
Cell dimensions, Å
a, b 61.1 61.1 61.0 61.0 60.9 61.2 61.5 61.1
c 96.8 96.8 97.0 97.1 96.9 96.3 97.7 96.3
Total reflections 40,327 33,301 53,978 28,398 39,326 30,082 105,345 33,225
Independent reflections 17,643 17,670 19,961 15,116 19,920  9,358 22,032 15,148
Rmerge, % 6.3 6.8 7.6 4.4 3.0 7.0 6.4 4.3
Resolution used 20–1.9 20–1.8 20–1.8 20–2.0 20–1.85 19–2.3 20–1.9 20–2.1
Reflections included 16,175 18,223 20,727 13,237 14,752  9,350 17,129 11,761
Completeness, %     92     88     95     87     78     96     95     89
Δbond length, Å 0.013 0.013 0.018 0.019 0.014 0.016 0.017 0.015
Δbond angle, ° 2.6 2.4 3.0 2.9 2.6 2.6 3.0 2.8
Δplanes, Å 0.010 0.011 0.014 0.015 0.012 0.017 0.014 0.012
R, % 16.5 16.5 16.7 16.5 15.5 18.4 16.9 16.6

WT* lysozyme crystallizes in space group P3221 with cell dimensions a = b = 61.2 Å, c = 96.8 Å (21). The crystals of all mutants are isomorphous. Rmerge gives the agreement between independently measured intensities while R is the crystallographic residual after refinement. Δbond lengths, Δbond angle, and Δplanes give, respectively, the average deviations of bond lengths, bond angles, and planar groups from their expected values. X-ray date also were measured for the double mutants E11H/T26H, D20C/T26D, and D20C/D26H. Preliminary analysis did not suggest anything unusual about these structures. They were not refined and are not included here.