Conservation and divergence between cytoplasmic and muscle-specific actin capping proteins: insights from the crystal structure of cytoplasmic Cap32/34 from Dictyostelium discoideum

Table 1 Crystallographic statistics

	Cap32/34
Data Collection
Space Group	P4₁
Cell Dimensions
a, b, c (Å)	124.5, 124.5, 77.5
α, β, γ (º)	90, 90, 90
Resolution Range (Å)	50-2.2 (2.3-2.2)
Number of Reflections	367874
Number of Unique Reflections	60185
Completeness (%)	99.8 (99.6)
Multiplicity
R _merge ^†	14.9 (83.5)
<I/σI>	14.2 (3.8)
Refinement
R _work ^‡	0.226
R _free ^§	0.265
R.m.s. deviations
Bond lengths (Å)	0.008
Bond angles (°)	1.36
Ramachandran Analysis
Residues in most favoured regions (%)	95.9
Residues in allowed regions (%)	4.1
Outliers (%)	0
Model statistics
Protein residues:
No. in subunit A & B	514
B-factor A & B (Å²)	15.4
Additional groups:
Water (No. / B-factor)	328 / 37.9

Values in parentheses refer to the highest resolution shell.
^†R_merge = Σ_hklΣ_i| I_i(hkl) - < I(hkl) > |/ Σ_hklΣ_iI_i(hkl); where I_i(hkl) is the intensity of the i th measurement of reflection hkl and < I(hkl) > is the mean value of I_i(hkl) for all i measurements.
^‡R_work = Σ_hkl||F_o|-|F_c||/Σ|F_o|, where F_o is the observed structure factor and F_c is the calculated structure factor.
^§R_free is the same as R_cryst except calculated with a subset, 5%, of data that are excluded from refinement calculations.

ISSN: 1472-6807