Compact HomeLab™
A turnkey, low maintenance single crystal X-ray diffraction system for protein and macromolecular crystallography, the Rigaku Compact HomeLab enables crystal screening through complete protein structure solution in a small-footprint, energy-efficient package.
Microfocus sealed tube X-ray source
The foundation of this system is the Rigaku MicroMax™-002+,
an integrated microfocus sealed tube generator and specialized
confocal optic. This system employs a uniquely small focal spot that
leads to an intense, monochromatic beam on the sample, resulting in better
data and higher signal-to-noise for small protein crystals. For 100 micron samples, usable flux produced by the Compact HomeLab is up to 3 times greater than that of a fine focus (0.3 mm) rotating anode generator and
Blue optic, and 5 times greater than that of a conventional sealed tube source with multilayer optics
(see comparison
graph). The Compact HomeLab's small,
intense beam enables the screening and collection of
quality data from small protein crystals on a low-maintenance X-ray system
in the home laboratory.
CCD or IP area X-ray detector
The Compact HomeLab can be equipped with a state-of-the-art CCD or Imaging Plate (IP) detector. Rigaku-manufactured detectors are fully integrated with the MicroMax-002+ to allow high-resolution protein data collection. A Rigaku R-AXIS IP detector is ideal for small or poorly diffracting crystals requiring long exposure times, and for crystals with long unit cells that require long crystal-to-detector distances. The Rigaku Saturn 944+ CCD detector is an excellent choice for fast data collection and also a great detector for screening samples.
|
Source: |
MicroMax-002+ microfocus sealed tube generator and CMF optic |
|
Detector: |
R-AXIS IV++
two-IP system |
|
Single φ vertical or 3-axis
partial χ goniometer for R-AXIS detectors |
|
|
Software: |
CrystalClear™
for data collection and processing |
Application notes
Request the following Compact HomeLab application notes by clicking on the links below:
- MicroMax-002+: Microfocus sealed tube X-ray source performance
- MicroMax-002+: Example of macromolecular crystallography data
Customer experiences
The following documents serve to illustrate customer experiences with the Compact HomeLab system or its subcomponents:
- Miller M and Deacon A. An X-ray microsource based system for crystal screening and beamline development during synchrotron shutdown periods. Nuclear Inst. and Methods in Physics Research, A. 2007; 582(1): 233-5.
- Illustration of the MicroMax-002 as a beamline downtime X-ray source replacement at the Stanford Synchrotron Reasearch Laboratory (SSRL).
Reference papers
The following selected scientific papers serve to illustrate the performance capabilities of the Compact HomeLab system or its subcomponents:
- Lee C, Kuo C, Hsu M, Liang P, Fang J, Shie J, and Wang A. Structural basis of mercury- and zinc-conjugated complexes as SARS-CoV 3C-like protease inhibitors. FEBS Letters. 2007; 581(28): 5454-8.
- Chin C, Ko T, Lin T, Chou C, Chen C, and Wang A. Probing the DNA kink structure induced by the hyperthermophilic chromosomal protein Sac7d. Nucleic Acids Res. 2005; 33(1): 430-8.
- Ficko-Blean E and Boraston A. Cloning, recombinant production, crystallization and preliminary X-ray diffraction studies of a family 84 glycoside hydrolase from Clostridium perfringens. Acta Cryst. 2005; F61: 834-6.
- Huang K, Liu Y and Wang A. Cloning, expression, characterization, and crystallization of a glutaminyl cyclase from human bone marrow: A single zinc metalloenzyme. Protein Expression and Purification. 2005; 43(1): 65-72.
- Mayer M. Crystal structures of the GluR5 and GluR6 ligand binding cores: Molecular mechanisms underlying kainate receptor selectivity. Neuron. 2005; 45(4): 539-552.
- Huang K, Ko T, Hung C, Chu J, Wang A, and Chiou S. Crystal structure of a platelet-agglutinating factor isolated from the venom of Taiwan habu (Trimeresurus mucrosquamatus). Biochemcal Journal. 2004; 378(2): 399-407.
- Huang W, Ko T, Li S and Wang A. Crystal structures of the human SUMO-2 protein at 1.6 Å and 1.2 Å resolution: implication on the functional differences of SUMO proteins. European Journal of Biochemistry. 2004; 271(20): 4114-22.


