“All we have discovered is that it starts with a single individual – always a child – and then spreads explosively, like the formation of crystals round the first nucleus in a saturated solution.” Arthur C. Clarke (Childhood’s End, 1953)


Our customer service approach is straightforward: we strive to be friendly, respectful, and professional in every interaction. All users—whether from Johns Hopkins University or external institutions—receive the same high standard of service.

We are committed to providing expert guidance, high-quality results, and timely feedback on submitted samples. Services can be tailored to meet specific research needs, and we welcome submissions from both academic and non-academic institutions. Confidentiality agreements can be arranged upon request. For non-JHU users, please contact the X-ray Facility Manager at [email protected] to discuss your requirements and obtain a cost estimate. We also actively welcome opportunities for scientific collaboration.

Services


  • Small-Molecule Crystallography
    Single-crystal X-ray diffraction analysis and full structure determination of a wide range of compounds, including organic, inorganic, organometallic, coordination complexes, and metal–organic frameworks (MOFs).
  • Protein Crystallography
    Crystal screening and optimized X-ray data collection for protein crystals
  • Specialized Sample Handling
    Expertise with air-, moisture-, and temperature-sensitive samples.
  • Crystal Quality Assessment
    Inspection under a polarizing stereo microscope; evaluation under a nitrogen cold stream for unstable samples.
  • Database Searches
    Identification of known compounds via the Cambridge Structural Database (CSD).
  • Low-Temperature Data Collection
    Standard measurements at 110 K using either Mo Kα or Cu Kα radiation; redundant data typically 6–10-fold (higher redundancy available on request).
  • Variable-Temperature Studies
    Semi-automated measurement of unit cell parameters and crystal structures across a controlled temperature range of 100–300 K (precision ± 0.1 K). These studies enable the investigation of temperature-dependent structural changes, such as phase transitions, thermal expansion/contraction, and variations in molecular packing, providing valuable insights into material stability and behavior under different thermal conditions.
  • Crystal Imaging
    Recording of JPEG crystal movies, useful for crystal face indexing.
  • Absorption Corrections
    Analytical numeric absorption correction using multifaceted crystal models.
  • Structure Determination
    Comprehensive structure solution and refinement, including challenging cases such as disordered, twinned, high-Z′, pseudosymmetric, and commensurately modulated structures.
  • Absolute Structure Determination
    Determination of absolute configuration for enantiopure compounds, including those composed exclusively of light atoms (e.g., molecules containing only oxygen as the heaviest atom).
  • Special Topics of Interest
    Polymorphism (screening and analysis), solid–solid phase transitions, solvates, and co-crystals.
  • Final Deliverables
    Edited CIF file, experimental report, ORTEP plot(s), data files, and supporting documentation.
  • Consulting and Support
    Expert advice, consultancy, and interpretation of structural results.

Pricing


(as of 09/02/2025)
JHU
non-JHU Academic
non-Academic
Package I
$10.00 per hour
$15.00 per hour
$40.00 per hour
Package II
$30.00
$37.00
$106.00
Package III
$122.00
$138.00
$318.00
Package IV
$249.00
$292.00
$716.00

Package I
This package covers crystal screening and is limited to protein X-ray crystallography. The purpose of crystal screening is to:
(i) Distinguish whether the sample is a protein crystal or a salt.
(ii) Assess the diffraction quality, including the maximum achievable resolution.
Note: Unit cell determination is not included in this package.

Package II
This package includes unit cell determination and optional crystal face indexing. Diffraction intensities are typically measured at 110 K (adjustable between 80–400 K if required). A CSD (Cambridge Structural Database) search can be typically performed to determine whether the crystal structure has been previously reported or is novel. Results and supporting files are delivered via email the same day.
Expected workload: typically under 15 minutes.

Package III
This package builds on Package II, adding data collection/reduction and analytical absorption corrections. Crystal face indexing is also included. Intensities are typically measured at 110 K (adjustable between 80–400 K if required). Data are collected to a resolution of 0.77–0.84 Å, or higher if necessary. Results, including the .HKL data file and additional files, are provided via email within the same (or next) business day.
Expected workload: same business day; next business day at the latest.

Package IV
This package includes everything in Package III, plus structure solution and refinement. A finalized set of results and files is provided as a ZIP package via email.
Expected workload: same day for straightforward structures, several days for more complex or challenging cases.