Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD

Table 1 X-ray data-collection and refinement statistics

	SycD_21-163/YopD
Data collection
Wavelength (Å)	0.918
Space group	P 3₁21
Unit cell parameters
a, b, c (Å)	106.4, 106.4, 52.0
α, β, γ (°)	90, 90, 120
Resolution range (Å)	25–2.5 (2.64-2.5)
No. observed/unique reflections	166476/11931
Completeness	99.4 (97.0)
Multiplicity	14.0 (10.0)
R_merge (%)^*	10.6 (57.1)
Mean I/σ(I)	18.5 (3.1)
Wilson B factor (Å²)	79.6
Refinement
R_work/R_free (%)^§	19.0/23.8 (31.3/34.8)
Mean B factor (Å²)
Overall	79.2
Protein	78.1
Peptide	84.0
Ligand/ion	105.3
Water	75.3
No. of atoms
Protein/peptide	1127
Ligand/ion	35
Water	17
R.m.s.d.
bond (Å)	0.007
angle (°)	1.061
Ramachandran
favored (%)	95.6
allowed (%)	4.4

$* R_{merge} = \sum_{hkl} \sum_{i} | I_{i} (h k l) - I 〈 (h k l) 〉 | / \sum_{hkl} \sum_{i} I_{i} (h k l)$ where I_i(hkl) is the i th measurement of the reflection (hkl).
^§ $R_{work} / R_{free} = \sum_{hkl} | | F_{obs} | - | F_{calc} | | / \sum_{hkl} | | F_{obs} | |$ . R_work was calculated from the work set. R_free was calculated from the test set encompassing 4.9% of the total reflections. The test set was not used in refinement. Values in parentheses belong to the highest resolution shell.

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