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Protein crystallization and characterization

At the LP3 crystallization and biophysical laboratory, users can carry out a wide variety of robot-assisted crystallization experiments in nanovolumes as well as screen for a large number of buffer conditions to stabilize their sample. LP3 has been granted beamtime at BioMAX (the X-ray macromolecular crystallography beamline of MAX IV). This allows users to have their crystals rapidly evaluated for diffraction and with the funding from BioCARE (a governmental supported strategic research area in cancer) the LP3 can also offer the possibility to process data and solve structures.



  • Mosquito LCP nanolitre pipetting robot (TTP Labtech)
    Allows the setting up of crystallization drops with volumes as low as 50 nl protein + 50 nl reservoir. Can set up 1–3 protein drops per reservoir, thus 96–288 experiments per plate. Can also set up LCP (lipidic cubic phase).
  • Oryx8 (Douglas instruments)
    Protein crystallization robot for sitting drop and microbatch screening and optimization, including seeding experiments.
  • Minstrel HT UV imaging system (Rigaku)
    Images the crystallization experiments at high resolution using visible and UV illumination. The latter allows the identification of even very small crystals hidden in precipitate, or discrimination of protein crystals from salt. Images are available to users over the Internet through the CrystalTrak software.

Biophysical characterization

  • Mx3005P qPCR system (Stratagene)
    Used for studying the thermal unfolding of proteins using the Thermofluor technique, otherwise known as differential scanning fluorimetry (DSF). Typically we use this to probe the effect of buffer conditions and additives on protein stability, which is useful in preparation for a crystallization experiment.
  • Zetasizer APS dynamic light scattering system (DLS) (Malvern)
    Used to study the aggregation state of proteins.
  • Prometheus NT.48 (Nanotemper)
    Differential scanning fluorimetry (DSF) without the need to add dyes or other compounds to the protein sample.

Available crystallization screens

From Molecular Dimensions

  • Basic Chemical Space screen (BCS)
  • JCSG+
  • MemStart & MemSys
  • Memgold
  • MemMeso
  • Morpheus
  • PACT Premier
  • ProPlex
  • SG1    
  • Structure Screen 1+2
  • Stura Footprint / MacroSol

From Hampton Research

  • Additive Screen
  • Detergent Screen

We are constantly seeking to improve our service, so if there is a crystallization screen that you miss here, please let us know (well in advance) and we will try to provide it.

DSF Screens

From Molecular Dimensions

  • Durham pH screen
  • Durham salt screen
  • Rubic additive screen
  • Rubic buffer screen

Booking, manuals and rules for use

The crystallization facility is available after booking. Please contact Maria [dot] Gourdon [at] biol [dot] lu [dot] se to book an instrument. We appreciate if you book a few days in advance.

Instrument availability can be checked using Google calendar, see link on the right hand side.

You will be required to fill in a sample sheet with the identity of your enzyme and other information.

If not stored by default in the Minstrel HT UV, your experiments can be set on marked shelves in the 12°C incubator and/or in the 4°C cold room.

For manuals, please use the download links on the right hand side.

Sending LP3 crystals for testing

Two weeks before beamtime (see dates below) please announce interest in sending your crystals to BioMAX. There will also be a reminder sent out via email to all users before the upcoming beamtime. You will be asked to fill out a form about your crystals (what to expect, space group etc) to facilitate the testing of your crystals. If you need help in fishing and flash freezing your crystals LP3 can assist you in that.

Beamtime at BioMAX: 23rd of March 2018, 4th of May 2018

Prices (applies for LU users only)

External users should contact us for pricing.

Price list

A typical screen might consist of two general 96-condition screens (e.g. PACT Premier and JCSG+) conducted at two temperatures (typically 20°C and 4°C). A typical drop size consists of 100 nl of protein and 100 nl of precipitant solution. Each screen requires 15 µl of macromolecule. At 10 mg/ml this represents only 0.15 mg of sample per screen.

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Contact information

The LP3 labs are located on floor 1 in Biology building A, Sölvegatan 35, Lund.

The Biology Building

Lund Protein Production Platform
Biology Building A
Sölvegatan 35

+46 46 2227785

lp3 [at] biol [dot] lu [dot] se

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LP3 acknowledges generous financial support from Lund University and BioCARE (A Strategic Research Area at Lund University).

LP3 and the former crystallization facility acknowledges past generous financial support from Lund University, Knut and Alice Wallenberg Foundation (SWEGENE programme), the Erik & Maja Lundqvist Foundation, the Carl Tesdorpf Foundation and the Swedish Research Council.