. Author manuscript; available in PMC: 2009 May 11.

Published in final edited form as: Biochemistry. 2009 Feb 24;48(7):1553–1561. doi: 10.1021/bi8022015

Table 2.

Least-Squares Refinement Statistics

Resolution Limits (Å)	30.0-2.15
^aR-factor (overall) %/no. reflections	21.5(60951)
R-factor (working) %/no. reflections	21.3(54989)
R-factor (free) %/no. reflections	26.9(5962)
No. Protein Atoms	5876^b
No. Hetero-atoms	280^c
Average B values (Å²)
Protein Atoms	50.6
PLP Derivatives	45.7
Solvents	45.2
Weighted RMS Deviations from Ideality
Bond Lengths (Å)	0.012
Bond Angles (deg)	2.32
Trigonal Planes (Å)	0.007
General Planes (Å)	0.013
^d Torsional Angles (deg)	19.5

R-factor = (Σ|F_o − F_c|/Σ|F_o|) × 100 where F_o is the observed structure-factor amplitude and F_c is the calculated structure-factor amplitude.

These include Glu 16, Tyr 17, and Gln 258 in subunit 1 and Asp 36 in subunit 2 adopting multiple conformations.

These include 2 PLP/dTDP-sugars and 180 waters.

The torsional angles were not restrained during the refinement.