Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapB (Rv2773c) from Mycobacterium tuberculosis.
Dihydrodipicolinate reductase from Mycobacterium tuberculosis (DapB, DHDPR, Rv2773c) has been cloned and heterologously expressed in Escherichia coli, purified using standard chromatographic techniques and crystallized in three different crystal forms. Preliminary diffraction data analysis suggests the presence of two tetramers in the asymmetric unit of one crystal form and half a tetramer in the other two crystal forms.
Kefala
Georgia
G
EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
Janowski
Robert
R
Panjikar
Santosh
S
Mueller-Dieckmann
Christoph
C
Weiss
Manfred S
MS
D016880:Anisotropy; D002845:Chromatography; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D050746:Dihydrodipicolinate Reductase / Q000737:chemistry* / Q000235:genetics; D009169:Mycobacterium tuberculosis / Q000378:metabolism*; D009841:Oligonucleotides / Q000737:chemistry; D014961:X-Ray Diffraction
D009841:Oligonucleotides; D050746:Dihydrodipicolinate Reductase