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. Author manuscript; available in PMC: 2009 Jan 1.

Published in final edited form as: Nat Struct Mol Biol. 2008 Jun 22;15(7):738–745. doi: 10.1038/nsmb.1448

Table 1.

Data collection, phasing and refinement statistics

Rtt109 (Δ130–179)–acetyl-CoA complex
Data collection
Space group	F432
Cell dimensions a, b, c (Å)	233.91, 233.91, 233.91
	Peak	Inflection

Wavelength (Å)	1.0072	1.0090
Resolution (Å)^a	50–3.1 (3.21–3.1)	50–3.3 (3.42–3.3)
R_sym	0.123 (0.414)	0.125 (0.394)
I/sI	51.1(14.5)	53.6 (16.5)
Completeness (%)	100 (100)	100 (100)
Redundancy	45.5(44.9)	46.8 (46.9)
Refinement
Resolution (Å)	15–3.1 (3.21–3.1)
No. reflections	18,820	15,549
R_work/R_free	0.194/0.258
No. atoms
Protein	2,893
AcCoA/Hg	51/2
Water	28
B-factors
Protein	37.7
Ligand/ion	64.1/37.8
Water	24.6
R.m.s. deviations
Bond lengths (Å)	0.0081
Bond angles (1)	1.48

^a

Values in parentheses are for the highest resolution shell.