Preliminary X-ray crystallographic study of methyltetrahydrofolate: corrinoid/iron sulfur protein methyltransferase from Clostridium thermoaceticum.
Methyltetrahydrofolate:corrinoid/iron sulfur protein methyltransferase from Clostridium thermoaceticum has been crystallized in two polymorphic forms and characterized by X-ray diffraction measurements. Form I displayed orthorhombic symmetry with a = 63.9, b = 53.8, c = 164.0 A. Form II also displayed orthorhombic symmetry with a = 63.5, b = 87.1, c = 117.9 A. Crystals of form I diffract to approximately. 3 A resolution; those of form II diffract to approximately 2.7 A.
Department of Chemistry, University of Nebraska-Lincoln, 68588-0304, USA.
T I
TI
Doukov
S
S
Zhao
C R
CR
Ross
D L
DL
Roberts
J J
JJ
Kim
S W
SW
Ragsdale
J J
JJ
Stezowski