Table 1.

Data collection and refinement statistics for GDPMK wild type and its mutants

Crystal	wt + tartrate	D152A plus GDP-mannose	E100A (grown for 3 weeks)	E100A plus GDP-mannose (grown for 24 hrs)
Space group	C2221	P212121	P212121	P21
Cell dimensions	a = 75.3 Å	a = 58.9 Å	a=60.3	a=54.2
	b = 103.2 Å	b = 69.3 Å	b=69.2	b=55.8
	c = 254.5 Å	c = 99.6 Å	c=98.5	c=158.1
	α=b=γ = 90°	α=b=γ = 90°	α=b=γ = 90°	α=γ = 90°
				b=91.7
Data Collection Statistics
Wavelength (Å)	0.9809		1.54	0.9787
Resolution(Å)	30.0-2.5	50.0-2.03	50.0-2.1	50.0-2.45
(HighRes shell)a	(2.54-2.50)	(2.10-2.03)	(2.18-2.10)	(2.49-2.45)
Measured Reflect.	240,244	161,406	134,487	104,724
Unique Reflections	33,433	26,521	23,871	32,636
I/σ	28.6 (2.9)	40.7 (6.4)	30.1 (5.2)	17.8 (4.4)
Completeness (%)	96.4 (80.7)	98 (98.1)	96 (75.1)	93 (59.0)
Rsym/Rmerge (%)b	6.9 (34.4)	7.7 (37.7)	8.9 (33.1)	9.8(16.5)
Refinement
Rcryst (%)	0.21	0.23	0.20	0.22
Rfree	0.28	0.30	0.28	0.29
R.m.s deviations
Bond length (Å)	0.015	0.014	0.011	0.014
Angle (°)	1.5	1.4	1.3	1.6
Monomer in ASU	5	2	2	4
Total Atoms	7420	3343	3342	6246
Protein atoms	7153	2987	2943	5971
Water molecules	197	329	375	112
Ligand	Na+, Cl−, Tartrate	Mg2+, Cl−, PEG, Tris	Mg2+, PEG, Na+, Cl−	Mg2+, GDP-mannose, Na+, Cl−
Bfactor (protein)Å2	44.4	33.2	24.0	46.2
Bfactor (ligand) Å2	65.1	49.5	42.7	52.7
Bfactor (H20) Å2	41.6	39.6	31.0	45.4
Ramachandran(MF, allowed) % c	87.1, 100	88.4, 100	89.8, 99.4	88.6, 99.7
PDB Accession Code	3O52	3O6Z	3O69	3O61

^aData in parentheses correspond to the outer resolution shell.

^bR_sym=Σ_hklΣ_J|I_j-<I>|/Σ_hklΣ_J I_j where <I> is the mean intensity of j observations from a reflection hkl and its symmetry equivalents.

^cMF=Percentage of residues in most favorable region allowed= Percentage of residues in allowed region