Biological Materials

Man working in science lab, Fraden Lab 

The Biological Materials Facility (BMF) supports MRSEC through the production of biological materials and training of MRSEC members as well as collaborators. The BMF is equipped to conduct expression, purification, and biochemical/biophysical analysis of proteins and protein complexes used by both the Membrane-based Materials and Biological Active Materials interdisciplinary research groups. A variety of high-performance liquid chromatography tools are already available and will grow to suit the needs of BMF clients.

Clients are welcome and encouraged to participate in these activities either under supervision of BMF staff or independently with demonstrated competence. Consulting is also available on design, conduct, and interpretation of any research involving biological materials. These services are also accessible to users outside of MRSEC or Brandeis University who can provide their own consumables. 

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Available Resources and Services


We offer the following equipment. Please contact Dr. Marc Ridilla for access or more information.


1. Shaking incubators (total shaken flask capacity 17 x 2 L)

a. Excella E25 - no refrigeration, 10 x 2 L
b. Innova 4230 - refrigerated - any temp, 3 x 2 L, also shelf for plates
c. Barnstead MaxQ 4000 A-Class - in the cold room, 4 x 2 L

2. Stationary incubators - 2 x VWR, shelves, no movement

3. Fermenter - New Brunswick BioFlo 320

     Working volume range: 0.6-1.9 L (0.25-40 L with a user-supplied single-use vessel (∼$500))


1.  Centrifuges

a. Beckman Optima TL (100,000 RPM)
b. Beckman Avanti J-30I (30,000 RPM)
c. Beckman Optima XE-90 (90,000 RPM)
d. Sorvall Legend RT (15,000 RPM)

2.  Rotors

Speed Capacity
a.  Type 45 Ti 235,000 x g 6 x 70 mL
b.  Type 90 Ti 694,000 x g 8 x 13.5 mL
c.  JA-30.50 Ti 108,860 x g 8 x 50 mL
d.  JA-10 17,700 x g 6 x 500 mL
e.  TLA 100.4 543,000 x g 8 x 5.1 mL
f.  Heraeus 6445 3,716 x g 4 x 750 mL

Protein Purification

a. AKTA Pure Chromatograph
b. Unicorn 6.4 control software
c. UV (280 nm) absorbance detector
d. F9-R fraction collector (175 x 12 mm tubes or 95 x 18 mm tubes)
e. Pre-packed columns:

Name Cat. # Volume (mL)
Capacity Flow Rate (mL/min)
Pressure Limit (MPa)
SEC Optimal Separation (kDa)
HiTrap Chelating HP 17-0409-01 5 60 mg 5 0.5
HiTrap SP HP 17-1151-01 1 55 mg 1 0.5
HiTrap Q HP 17-1153-01 1 50 mg 1 0.5
HiTrap Q HP 17-1154-01 5 250 mg 5 0.5
Hi-Prep 16/60 Sephacryl S-200 HR 17-1166-01 120 5 mL 0.5 0.15 5-250
Hi-Prep 16/60 Sephacryl S-300 HR 17-1167-01 120 5 mL 0.5 0.15 10-500
HiTrap Desalting 17-1408-01 5 1.5 mL 1 0.5
HiTrap Q FF 17-5053-01 1 120 mg 1 0.5
HiTrap DEAE Sepharose FF 17-5154-01 5 550 mg 5 0.5
HiTrap Q FF 17-5156-01 5 600 mg 5 0.5
MonoQ 5/50 GL 17-5166-01 1 50 mg 0.5 4
Superdex 75 10/300 GL 17-5174-01 24 10 mg / 500 μL 0.5 1.8 3-70
HiTrap Phenyl FF (High Sub) 17-5193-01 5 200 μmol 5 0.5
HisTrap HP 17-5247-01 1 40 mg 1 0.5
HiTrap TALON crude 28-9537-67 5 100 mg 5 0.5
Superdex 200 Increase 10/300 GL 28-9909-44 25 10 mg / 500 μL 0.5 5 10-600

ALV/DLS/SLS-5000 Light Scattering System

     View the ALV Manual and Software Screenshots

Cold Room Bench Space

Materials Production

MRSEC investigators have developed a number of biologically inspired experimental model systems, ranging from microtubule based active matter1-5 to colloidal membranes6-9. BMF supports MRSEC investigations of active and soft matter through large-scale production of the cells, proteins, and viruses. We are now extending this service to the broader community including extramural labs. BMF wants to help you get started studying biological material in your own lab by supplying samples and/or training you to make your own. Outside investigators are welcome to visit. 

Currently ongoing production

  • Cells: E. coliSalmonella
  • Purified proteins:  microtubules, kinesins, flagella
  • Purified filamentous bacteriophages: fd, M13
Active Matter
A great deal of interest has arisen in the material properties of the "Active Matter" advanced by Brandeis MRSEC's own Dogic lab. This mixture of purified microtubules, kinesin, and a minimal set of supporting chemicals yields a self-pumping gel with unique properties and numerous potential applications. We want to help you get started studying this material in your own lab by supplying a small amount of sample and/or training you to make your own. 

Analytical Ultracentrifugation (MRSEC / Gelles Lab Shared Equipment)

1. What can I learn from AU (in order of decreasing probability)?

  • Is the sample homo- or heterogeneous?
  • How many different components are present in the sample?
  • Does the sample exhibit significant concentration dependency in S for the concentration range under which you investigate?
  • Does the sample self-associate?
  • Does the sample aggregate, and if so, by how much?
  • What are the relative and partial concentrations of each component?
  • Is the aggregation/association reversible?
  • Do two different components in the system interact and bind?
  • What is the stoichiometry of this interaction?
  • What is the range of S-values?
  • For homogeneous solutions: what is the approximate diffusion coefficient?
  • For paucidisperse solutions: while exact determination of diffusion coefficients becomes increasingly more difficult with additional components in the system, for some well-conditioned cases this is possible, at least qualitatively
  • Does the sample change composition over time, i.e., does the sample undergo degradation or aggregation during the sedimentation process?
  • Does the sample undergo conformational changes?

2. Available Instrumentation

Optima XL-A Centrifuge
An-60 Ti Rotor
Epon 2-channel and 6-channel cells

3. Requirements

a. Sedimentation Velocity - 400 μL sample at 0.5-1.0 AU (and 425 μL buffer)
b. Sedimentation Equilibrium - 110 μL sample at 0.1-0.5 AU (and 125 μL buffer)

Additional questions on ...
Circular dichroism spectroscopy - Is your protein folded? Check the CD spectrum!
Chemistry Department Jasco J-810 

Typhoon imager access

General fluorescence uses and techniques (intensity, anisotropy/polarization, FRET, etc.)

Protein structure visualization/modeling, docking