. Author manuscript; available in PMC: 2010 Jul 7.

Published in final edited form as: Biochemistry. 2009 Jul 7;48(26):6146–6156. doi: 10.1021/bi900663h

Table 1.

Data collection and refinement statistics for HICA variants^a

	W39F (PDB 3E24)	D44N (PDB 3E1V)	Y181F (PDB 3E28)	Y181F + 100 mM HCO₃⁻ (PDB 3E2A)
	Data collection statistics
Source	Rigaku RU-200	Oxford Diffraction PX Enhance Ultra	Rigaku RU-200	Rigaku RU-200
Wavelength (Å)	1.54	1.54	1.54	1.54
Space Group	I2₁2₁2₁	P4₃2₁2	C2	C2
Cell parameters (Å)	48.2, 129.6, 144.1	81.6, 81.6, 187.8	230.2, 144.9, 52.7	230.6, 145.5, 53.2
(°)	90, 90, 90	90, 90, 90	90, 93.8, 90	90, 93.8, 90
Resolution (Å)	29.5–2.30 (2.36-2.30)	29.2–2.80 (2.87-2.80)	29.8–2.50 (2.56-2.50)	24.7–2.30 (2.36-2.30)
Unique reflections	20243	16060	59536	77406
Redundancy	4.6 (4.3)	10.2	4.0 (4.0)	3.5 (3.4)
Completeness	98.7 (98.4)	98.6 (97.4)	99.9 (100)	100 (99.9)
R_sym (%)	0.059 (0.314)	0.093 (0.463)	0.090 (0.520)	0.065 (0.343)
〈I〉/〈σI〉^b	22.2 (4.4)	19.4 (4.1)	19.6 (2.6)	18.7 (3.6)
	Refinement statistics
Reflections in test set	1990	812	2984	7808
R_work (%)	0.191	0.194	0.206	0.205
R_free (%)	0.236	0.233	0.256	0.244
No. of atoms
Protein	2942	2890	9940	9906
Ligand	20	0	90	64
Ion	2	2	6	6
Solvent	138	21	172	158
rmsd from ideal^c
Bond distance (Å)	0.010	0.012	0.012	0.011
Bond angle (°)	1.2	1.3	1.3	1.2
Ramachandran plot outliers (%)^d	5.0	6.6	3.6	2.4

Values in parentheses represent data for the highest resolution shell.

Reported as 〈〈I〉/σ〈I〉〉 in SCALA or SCALEPACK.

Ideal values from Engh and Huber (50).

Calculated using a strict boundary Ramachandran plot (33).