Dear Niu,
It is very unlikely that MBP will be disordered. We use that protein a
standard for SAXS calibration and gel filtration it is extremely well
behaved.
There is an excellent review about MBP enhanced crystallization (by Moon et
al) and you can do a quick survey of the PDB to find the corn
Dear Randy,
Over the last ~6 years, we have tried to use the MBP tag to enhance
crystallization on >10 proteins. Only one that couldn't crystallize by
itself in the end crystallized with the fusion tag. However,
unfortunately, the target protein (~10 kDa) turned out to be in the big
cavity of the
Dear Niu,
When it works, crystallising a fusion protein can be great, with the big
advantage that placing a model for the (known) carrier protein gives free phase
information. Certainly there are examples of this working, but in the early
days of this (20 years or so ago?), I remember hearing
Hi Niu,
Several things come to mind. First, it may not be trivial when the first
component to be placed is ~20kDa and the second component (SU) is ~43kDa.
The signal after placing the first component may be weak. Also, if the
model for the smaller SU has low sequence identity with the target and y
Dear All,
Recently we collected some data of a MBP fusion protein, at around 4A
resolution. The protein itself is about half of the MBP size. However when
we tried to solve it with MR, it failed. We tried to use MBP alone,
homology model of target protein alone, and MBP+model. It is very strange
t
